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A compound of Compound 1 or Compound 96: (Compound 1) or (Compound 96) or an enantiomer, a mixture of enantiomers, a pharmaceutically acceptable form thereof. 2. The compound of claim 1, wherein the compound is: ound lr), (Compound 96s), or (Compound 96r), a mixture of enantiomers, a pharmaceutically acceptable form thereof. The compound of claim 1, wherein the compound is: (Compound 1 s) or (Compound 96s), or a mixture of enantiomers, a pharmaceutically acceptable form thereof. 4. The compound of claim 3, wherein the compound has an enantiomeric excess of greater than about 25%, greater than about 30%, greater than about 40%, greater than about 50%, greater than about 60%, greater than about 70%, greater than about 80%, greater than about 85%, greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%. 5. The compound of claim 4, wherein the enantiomeric excess is greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%. 6. The compound of claim 5, wherein the enantiomeric excess is greater than about 97%, greater than about 98%, or greater than about 99%. 7. The compound of any of claims 1 -6, wherein the pharmaceutically acceptable form is a salt or a solvate. 8. The compound of any of claims 1-7, wherein the pharmaceutically acceptable form is a salt. 9. The compound of any of claims 1-7, wherein the pharmaceutically acceptable form is a solvate. 10. A compound, wherein the compound is selected from a compound in Table 1, Table 2, Table 2, Table 3, Table 4, Table 5, or Table 6. 11. A pharmaceutical composition comprising a compound of any of claims 1-10, and a pharmaceutically acceptable excipient, diluent, or carrier. 12. A method of treating or preventing a PI3K mediated disorder in a subject, the method comprising administering a therapeutically effective amount of a compound of any of claims 1-10 or a composition of claim 11 to said subject. 13. Use of a compound of any of claims 1 - 10 in the manufacture of a medicament for treating or preventing a PI3K mediated disorder in a subject. 14. A compound of any of claims 1-10 for use in treating or preventing a PI3K mediated disorder in a subject. 15. The method, use, or compound of any of claims 12-14, wherein the disorder is cancer, an inflammatory disease, or an auto-immune disease. 16. A method for inhibiting PI3K in a cell or subject comprising contacting the cell or administering to the subject a compound of any of claims 1-10. 17. A process of preparing a (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising: deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one. 18. The process of claim 17, further comprising: contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- 1 (2H)-one with 6-chloro-9-(tetrahydro-2H- pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( IS)- 1 -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one. 19. The process of claim 18, further comprising: contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one. 20. The process of claim 19, further comprising: contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate. 21. A process of preparing a (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising: contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate; contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one; contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- 1 (2H)-one with 6-chloro-9-(tetrahydro-2H- pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( IS)- 1 -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one; and deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one. 22. A process of preparing 8-fluoro-2-phenyl-3-((lS)-l-((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one comprising contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- l(2H)-one with 6-chloro-9-(tetrahydro-2H-pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3-((lS)-l-((9- (tetrahydro-2H-pyran-2-yl)-9H-purin-6-yl)amino)propyl)isoquinolin-l(2H)-one.","lang":"en","source":"WIPO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"HETEROCYCLIC COMPOUNDS AND USES THEREOF [0001] This application claims priority to U.S. Provisional Application Nos. 61/893,813, filed October 21, 2013, and 62/003,457, filed May 27, 2014, the entireties of which are incorporated herein by reference. BACKGROUND [0002] The activity of cells can be regulated by external signals that stimulate or inhibit intracellular events. The process by which stimulatory or inhibitory signals are transmitted into and within a cell to elicit an intracellular response is referred to as signal transduction. Over the past decades, cascades of signal transduction events have been elucidated and found to play a central role in a variety of biological responses. Defects in various components of signal transduction pathways have been found to account for a vast number of diseases, including numerous forms of cancer, inflammatory disorders, metabolic disorders, vascular and neuronal diseases (Gaestel et al. Current Medicinal Chemistry (2007) 14:2214-2234). [0003] Kinases represent a class of important signaling molecules. Kinases can generally be classified into protein kinases and lipid kinases, and certain kinases exhibit dual specificities. Protein kinases are enzymes that phosphorylate other proteins and/or themselves {i.e., autophosphorylation). Protein kinases can be generally classified into three major groups based upon their substrate utilization: tyrosine kinases which predominantly phosphorylate substrates on tyrosine residues (e.g., erb2, PDGF receptor, EGF receptor, VEGF receptor, src, abl), serine/threonine kinases which predominantly phosphorylate substrates on serine and/or threonine residues (e.g., mTorCl, mTorC2, ATM, ATR, DNA-PK, Akt), and dual-specificity kinases which phosphorylate substrates on tyrosine, serine and/or threonine residues. [0004] Lipid kinases are enzymes that catalyze the phosphorylation of lipids. These enzymes, and the resulting phosphorylated lipids and lipid-derived biologically active organic molecules play a role in many different physiological processes, including cell proliferation, migration, adhesion, and differentiation. Certain lipid kinases are membrane associated and they catalyze the phosphorylation of lipids contained in or associated with cell membranes. Examples of such enzymes include phosphoinositide(s) kinases (e.g., PI3-kinases, PI4-kinases), diacylglycerol kinases, and sphingosine kinases. [0005] The phosphoinositide 3-kinases (PI3Ks) signaling pathway is one of the most highly mutated systems in human cancers. PI3K signaling is also a key factor in many other diseases in humans. PI3K signaling is involved in many disease states including allergic contact dermatitis, rheumatoid arthritis, osteoarthritis, inflammatory bowel diseases, chronic obstructive pulmonary disorder, psoriasis, multiple sclerosis, asthma, disorders related to diabetic complications, and inflammatory complications of the cardiovascular system such as acute coronary syndrome. [0006] PI3Ks are members of a unique and conserved family of intracellular lipid kinases that phosphorylate the 3 ' -OH group on phosphatidylinositols or phosphoinositides. The PI3K family comprises 15 kinases with distinct substrate specificities, expression patterns, and modes of regulation. The class I PI3Ks (pi 10a, ρΐ ΐθβ, ρΐ ΐθδ, and ρΐ ΐθγ) are typically activated by tyrosine kinases or G-protein coupled receptors to generate PIP3, which engages downstream effectors such as those in the Akt/PDKl pathway, mTOR, the Tec family kinases, and the Rho family GTPases. The class II and III PI3Ks play a key role in intracellular trafficking through the synthesis of PI(3)P and PI(3,4)P2. The PI3Ks are protein kinases that control cell growth (mTORCl) or monitor genomic integrity (ATM, ATR, DNA-PK, and hSmg-1). [0007] The delta (δ) isoform of class I PI3K has been implicated, in particular, in a number of diseases and biological processes. PI3K-6 is expressed primarily in hematopoietic cells including leukocytes such as T-cells, dendritic cells, neutrophils, mast cells, B-cells, and macrophages. PI3K-6 is integrally involved in mammalian immune system functions such as T-cell function, B-cell activation, mast cell activation, dendritic cell function, and neutrophil activity. Due to its integral role in immune system function, PI3K-6 is also involved in a number of diseases related to undesirable immune response such as allergic reactions, inflammatory diseases, inflammation mediated angiogenesis, rheumatoid arthritis, and auto-immune diseases such as lupus, asthma, emphysema and other respiratory diseases. SUMMARY [0008] Described herein are compounds capable of inhibiting one or more isoform(s) of class I PI3K. [0009] In one embodiment, provided herein is a compound of Compound 1 or Compound 96: (Compound 1), or (Compound 96), or an enantiomer, a mixture of enantiomers, a pharmaceutically acceptable form thereof. [0010] In one embodiment, the compound is: ound lr), (Compound 96s), or (Compound 96r) or a mixture of enantiomers, a pharmaceutically acceptable form thereof. [001 1 ] In one embodiment, the compound is: (Compound 96s), or a mixture of enantiomers, a pharmaceutically acceptable form thereof. [0012] In one embodiment, a compound provided herein (e.g., Compound Is or Compound lr) has an enantiomeric excess of greater than about 25%, greater than about 30%, greater than about 40%, greater than about 50%, greater than about 60%, greater than about 70%, greater than about 80%, greater than about 85%, greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%. In one embodiment, the enantiomeric excess is greater than about greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%. In one embodiment the enantiomeric excess is greater than about 97%, greater than about 98%, or greater than about 99%. [0013] In one embodiment, the pharmaceutically acceptable form of a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr) is a salt or a solvate. In one embodiment, the pharmaceutically acceptable form is a salt. In another embodiment, the pharmaceutically acceptable form is a solvate. [0014] In one embodiment, provided herein is a pharmaceutical composition comprising a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr), and a pharmaceutically acceptable excipient, diluent, or carrier. [0015] In one embodiment, provided herein is a method of treating or preventing a PI3K mediated disorder in a subject, the method comprising administering a therapeutically effective amount of a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr) or a composition thereof to said subject. [0016] In one embodiment, provided herein is a use of a compound provided herein (e.g., Compound 1 , Compound Is, or Compound lr) in the manufacture of a medicament for treating or preventing a PI3K mediated disorder in a subject. [0017] In one embodiment, provided herein is a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr) for use in treating or preventing a PI3K mediated disorder in a subject. In one embodiment, the disorder is cancer, an inflammatory disease, or an auto-immune disease [0018] In one embodiment, provided herein is a method for inhibiting PI3K in a cell or subject comprising contacting the cell or administering to the subject a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr). [0019] In one embodiment, as depicted in the scheme below, provided herein is a process of preparing a (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising: deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one. [0020] In one embodiment, as depicted in the scheme below, the process further comprising: contacting (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one with 6-chloro-9-(tetrahydro pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one. [0021] In one embodiment, as depicted in the scheme below, the process further comprising: contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one. NHBoc [0022] In one embodiment, as depicted in the scheme below, the process further comprising: contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate. NHBoc [0023] In one embodiment, provided herein is a process of preparing a (S)-3-(l-((9H-purin-6- yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising: contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate; contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one; contacting (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one with 6-chloro-9-(tetrahydro-2H- pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one; and deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one. [0024] In one embodiment, provided herein is a process of preparing 8-fluoro-2-phenyl-3-((lS)-l-((9- (tetrahydro-2H-pyran-2-yl)-9H-purin-6-yl)amino)propyl)isoquinolin- 1 (2H)-one comprising contacting (S)-3 -( 1 - aminopropyl)-8-fluoro-2-phenylisoquinolin- 1 (2H)-one with 6-chloro-9-(tetrahydro-2H-pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6-yl)amino)propyl)isoquinolin- 1 (2H)- one. [0025] In one embodiment, provided herein is a method of preparing a compound provided herein using a method provided herein. [0026] In certain embodiments, provided herein is a composition (e.g., a pharmaceutical composition) comprising a compound described herein and a pharmaceutically acceptable excipient. In some embodiments, provided herein is a method of inhibiting a PI3 kinase, comprising contacting the PI3 kinase with an effective amount of a compound or a pharmaceutical composition described herein. In certain embodiments, a method is provided for inhibiting a PI3 kinase wherein said PI3 kinase is present in a cell. The inhibition can take place in a subject suffering from a disorder selected from cancer, bone disorder, inflammatory disease, immune disease, nervous system disease (e.g., a neuropsychiatric disorder), metabolic disease, respiratory disease, thrombosis, and cardiac disease, among others. In certain embodiments, a second therapeutic agent is administered to the subject. [0027] In certain embodiments, a method is provided for selectively inhibiting a PI3 kinase delta isoform over PI3 kinase alpha or beta isoform wherein the inhibition takes place in a subject suffering from a disorder selected from cancer, bone disorder, inflammatory disease, immune disease, nervous system disease (e.g. , a neuropsychiatric disorder), metabolic disease, respiratory disease, thrombosis, and cardiac disease, said method comprising administering an effective amount of a compound or a pharmaceutical composition provided herein to said subject. In certain embodiments, provided herein is a method of treating a subject suffering from a disorder associated with PI3 kinase, said method comprising selectively modulating the PI3 kinase delta isoform over PI3 kinase alpha or beta isoform by administering an amount of a compound or a pharmaceutical composition provided herein to said subject, wherein said amount is sufficient for selective modulation of PI3 kinase delta isoform over PI3 kinase alpha or beta isoform. [0028] In certain embodiments, provided herein is a method of inhibiting a PI3 kinase in a subject, comprising administering to the subject an effective amount of a compound provided herein (e.g., a compound of Formula I, an inflammatory disease, an immune disease, or a respiratory disease. In one embodiment, the subject is a mammal. In one embodiment, the mammal is a human. In one embodiment, the subject is a human. [0029] In some embodiments, the disorder is a cancer. In one embodiment, the cancer is acute myeloid leukemia (AML), chronic myeloid leukemia (CML), myelodysplastic syndrome (MDS), myeloproliferative disorders, mast cell cancer, Hodgkin disease, non-Hodgkin lymphomas, diffuse large B-cell lymphoma, human lymphotropic virus type 1 (HTLV-1) leukemia/lymphoma, AIDS-related lymphoma, adult T-cell lymphoma, acute lymphocytic leukemia (ALL), T-cell acute lymphocytic leukemia, B-cell acute lymphoblastic leukemia, chronic lymphocytic leukemia, or multiple myeloma (MM). In one embodiment, the cancer is leukemia or lymphoma. In one embodiment, the leukemia is B-cell acute lymphoblastic leukemia (B-ALL), acute myeloid leukemia (AML), acute lymphocytic leukemia, chronic myeloid leukemia, hairy cell leukemia, myelodysplasia, myeloproliferative disorders, acute myelogenous leukemia (AML), chronic myelogenous leukemia (CML), chronic lymphocytic leukemia (CLL), multiple myeloma (MM), myelodysplastic syndrome (MDS), or mast cell cancer. In one embodiment, the lymphoma is diffuse large B-cell lymphoma, B-cell immunoblastic lymphoma, small non-cleaved cell lymphoma, human lymphotropic virus-type 1 (HTLV-1) leukemia/lymphoma, adult T-cell lymphoma, Hodgkin disease, or non-Hodgkin lymphomas. [0030] In some embodiments, the disorder is an inflammatory disease or an immune disease. In one embodiment, the inflammatory disease or the immune disease is asthma, emphysema, allergy, dermatitis, rheumatoid arthritis, psoriasis, lupus erythematosus, graft versus host disease, inflammatory bowel disease, eczema, scleroderma, Crohn's disease, or multiple sclerosis. In one embodiment, the disorder is rheumatoid arthritis. In one embodiment, the disorder is rheumatoid arthritis, and the amount of the compound is effective to ameliorate one or more symptoms associated with rheumatoid arthritis, wherein the symptom associated with rheumatoid arthritis is independently a reduction in the swelling of the joints, a reduction in serum anti collagen levels, a reduction in bone resorption, a reduction in cartilage damage, a reduction in pannus, or a reduction in inflammation. [0031] In some embodiments, the disorder is a respiratory disease. In one embodiment, the respiratory disease is asthma, chronic obstructive pulmonary disease (COPD), chronic bronchitis, emphysema, or bronchiectasis. In one embodiment, the disorder is asthma. [0032] In one embodiment, the method further comprises administration of one or more therapeutic agents selected from chemotherapeutic agents, cytotoxic agents, and radiation. In one embodiment, the compound is administered in combination with an mTOR inhibitor. In one embodiment, the compound is administered in combination with one or more of: an agent that inhibits IgE production or activity, 2-(4-(6-cyclohexyloxy-2- naphtyloxy)phenylacetamide)benzoic acid, an mTOR inhibitor, rapamycin, a TORC1 inhibitor, a TORC2 inhibitor, an anti-IgE antibody, prednisone, corticosteroid, a leukotriene inhibitor, XOLAIR, ADVAIR, SINGULAIR, or SPIRIVA. In one embodiment, the compound is administered in combination with one or more of: a mitotic inhibitor, an alkylating agent, an anti-metabolite, an intercalating antibiotic, a growth factor inhibitor, a cell cycle inhibitor, an enzyme, a topoisomerase inhibitor, an anti-hormone, an angiogenesis inhibitor, an anti-androgen, or an anti-receptor kinase antibody. In one embodiment, the compound is administered in combination with one or more of: Imatinib Mesylate, bortezomib, bicalutamide, gefitinib, ADRIAMYCIN, alkylating agents, alkyl sulfonates, ethylenimines, altretamine, triethylenemelamine, trietylenephosphoramide, triethylenethiophosphaoramide, trimethylolomelamine, nitrogen mustards, chlorambucil, chlornaphazine, cholophosphamide, estramustine, ifosfamide, mechlorethamine, mechlorethamine oxide hydrochloride, melphalan, novembichin, phenesterine, prednimustine, trofosfamide, uracil mustard, nitrosureas, antibiotics, anti-metabolites, denopterin, methotrexate, pteropterin, trimetrexate, 5-fluorouracil (5-FU), fludarabine, 6-mercaptopurine, thiamiprine, thioguanine, ancitabine, azacitidine, 6-azauridine, carmofur, cytarabine, dideoxyuridine, doxifluridine, enocitabine, floxuridine, androgens, anti-adrenals, folic acid replenisher, arabinoside, cyclophosphamide, thiotepa, taxanes, anti-hormonal agents, anti- estrogens, tamoxifen, raloxifene, aromatase inhibiting 4(5)-imidazoles, 4-hydroxytamoxifen, trioxifene, keoxifene, onapristone, toremifene, anti-androgens, chlorambucil, gemcitabine, 6 -thioguanine; mercaptopurine; cisplatin, carboplatin, vincristine; vinorelbine, vinblastin, ifosfamide, mitomycin C, daunorubicin, doxorubicin, mitoxantrone, HERCEPTIN, AVASTIN, ERBITUX, RITUXAN, TAXOL, ARIMIDEX, TAXOTERE, or an anti-receptor tyrosine kinase antibody selected from cetuximab, panitumumab, trastuzumab, anti CD20 antibody, rituximab, tositumomab, alemtuzumab, bevacizumab, and gemtuzumab. In one embodiment, the compound is administered in combination with one or more of: bortezomib, ADRIAMYCIN, alkylating agents, anti-metabolites, denopterin, pteropterin, trimetrexate, a nitrogen mustard, chlorambucil, chlornaphazine, cholophosphamide, estramustine, ifosfamide, mechlorethamine, mechlorethamine oxide hydrochloride, melphalan, novembichin, phenesterine, prednimustine, trofosfamide, uracil mustard, methotrexate, fludarabine, 6-mercaptopurine, thiamiprine, thioguanine, ancitabine, azacitidine, 6-azauridine, carmofur, cytarabine, dideoxyuridine, doxifluridine, enocitabine, floxuridine, androgens, cyclophosphamide, taxanes, anti-hormonal agents, gemcitabine; cisplatin, carboplatin, vincristine, vinorelbine, vinblastin, ifosfamide, mitomycin C, daunorubicin, doxorubicin, mitoxantrone, HERCEPTIN, AVASTIN, ERBITUX, RITUXAN, TAXOL, ARIMIDEX, or TAXOTERE. In one embodiment, the compound is administered in combination with one or more of: non-steroidal anti-inflammatory drugs (NSAIDs), corticosteroids, prednisone, chloroquine, hydroxychloroquine, azathioprine, cyclophosphamide, methotrexate, cyclosporine, anti-CD20 antibodies, ENBREL, REMICADE, HUMIRA, AVONEX, or REBIF. [0033] In one embodiment, provided herein is a method of inhibiting a PI3 kinase in a subject suffering from a cancer, comprising administering to the subject an effective amount of a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr). In one embodiment, the cancer is selected from acute myeloid leukemia (AML), chronic myeloid leukemia (CML), myelodysplastic syndrome (MDS), myeloproliferative disorders, mast cell cancer, Hodgkin disease, non-Hodgkin lymphomas, diffuse large B-cell lymphoma, human lymphotropic virus-type 1 (HTLV-1) leukemia/lymphoma, AIDS-related lymphoma, adult T-cell lymphoma, acute lymphocytic leukemia (ALL), B-cell acute lymphoblastic leukemia, T-cell acute lymphoblastic leukemia, chronic lymphocytic leukemia, or multiple myeloma (MM). In one embodiment, the cancer is leukemia or lymphoma. In one embodiment, the leukemia is selected from B-cell acute lymphoblastic leukemia (B-ALL), acute lymphocytic leukemia, hairy cell leukemia, myelodysplasia, myeloproliferative disorders, acute myelogenous leukemia (AML), chronic myelogenous leukemia (CML), chronic lymphocytic leukemia (CLL), multiple myeloma (MM), myelodysplastic syndrome (MDS), or mast cell cancer. In one embodiment, the lymphoma is selected from diffuse large B-cell lymphoma, B-cell immunoblastic lymphoma, small non-cleaved cell lymphoma, human lymphotropic virus-type 1 (HTLV-1) leukemia/lymphoma, AIDS-related lymphoma, adult T-cell lymphoma, Hodgkin disease, or non-Hodgkin lymphomas. In one embodiment, the compound is administered in combination with one or more therapeutic agents provided herein. [0034] In one embodiment, provided herein is a method of inhibiting a PI3 kinase in a subject suffering from an inflammatory disease or an immune disease, comprising administering to the subject an effective amount of a compound provided herein (e.g., Compound 1, Compound Is, or Compound lr). In one embodiment, the inflammatory disease or immune disease is asthma, emphysema, allergy, dermatitis, rheumatoid arthritis, psoriasis, lupus erythematosus, graft versus host disease, inflammatory bowel disease, eczema, scleroderma, Crohn's disease, or multiple sclerosis. In one embodiment, the inflammatory disease or immune disease is rheumatoid arthritis. In one embodiment, the compound is administered in combination with one or more therapeutic agents provided herein. [0035] In one embodiment, provided herein is a method of inhibiting a PI3 kinase in a subject suffering from a respiratory disease, comprising administering to the subject an effective amount of a compound provided herein (e.g. , a compound of Formula I). In one embodiment, the respiratory disease is asthma, chronic obstructive pulmonary disease (COPD), chronic bronchitis, emphysema, or bronchiectasis. In one embodiment, the respiratory disease is asthma. In one embodiment, the compound is administered in combination with one or more therapeutic agents provided herein. [0036] In certain embodiments, provided herein is a reaction mixture comprising a compound described herein. [0037] In certain embodiments, provided herein is a kit comprising a compound described herein. INCORPORATION BY REFERENCE [0038] All publications, patents, and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication, patent, or patent application was specifically and individually indicated to be incorporated by reference. In case of conflict, the present application, including any definitions herein, will control. DETAILED DESCRIPTION [0039] In one embodiment, provided are heterocyclyl compounds, and pharmaceutically acceptable forms thereof, including, but not limited to, salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives thereof. [0040] In another embodiment, provided are methods of treating and/or managing various diseases and disorders, which comprises administering to a patient a therapeutically effective amount of a compound provided herein, or a pharmaceutically acceptable form (e.g., salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives) thereof. Examples of diseases and disorders are described herein. [0041] In another embodiment, provided are methods of preventing various diseases and disorders, which comprises administering to a patient in need of such prevention a prophylactic ally effective amount of a compound provided herein, or a pharmaceutically acceptable form (e.g., salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives) thereof. Examples of diseases and disorders are described herein. [0042] In other embodiments, a compound provided herein, or a pharmaceutically acceptable form (e.g., salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives) thereof, is administered in combination with another drug (\"second active agent\") or treatment. Second active agents include small molecules and large molecules (e.g., proteins and antibodies), examples of which are provided herein, as well as stem cells. Other methods or therapies that can be used in combination with the administration of compounds provided herein include, but are not limited to, surgery, blood transfusions, immunotherapy, biological therapy, radiation therapy, and other non-drug based therapies presently used to treat, prevent or manage various disorders described herein. [0043] Also provided are pharmaceutical compositions (e.g., single unit dosage forms) that can be used in the methods provided herein. In one embodiment, pharmaceutical compositions comprise a compound provided herein, or a pharmaceutically acceptable form (e.g., salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives) thereof, and optionally one or more second active agents. [0044] While specific embodiments have been discussed, the specification is illustrative only and not restrictive. Many variations of this disclosure will become apparent to those skilled in the art upon review of this specification. [0045] Unless defined otherwise, all technical and scientific terms used herein have the same meaning as is commonly understood by one of skill in the art to which this specification pertains. [0046] As used in the specification and claims, the singular form \"a\", \"an\" and \"the\" includes plural references unless the context clearly dictates otherwise. [0047] As used herein, and unless otherwise indicated, the term \"about\" or \"approximately\" means an acceptable error for a particular value as determined by one of ordinary skill in the art, which depends in part on how the value is measured or determined. In certain embodiments, the term \"about\" or \"approximately\" means within 1, 2, 3, or 4 standard deviations. In certain embodiments, the term \"about\" or \"approximately\" means within 50%, 20%, 15%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 0.5%, or 0.05% of a given value or range. [0048] As used herein, \"agent\" or \"biologically active agent\" or \"second active agent\" refers to a biological, pharmaceutical, or chemical compound or other moiety. Non-limiting examples include simple or complex organic or inorganic molecules, a peptide, a protein, an oligonucleotide, an antibody, an antibody derivative, an antibody fragment, a vitamin, a vitamin derivative, a carbohydrate, a toxin, or a chemotherapeutic compound, and metabolites thereof. Various compounds can be synthesized, for example, small molecules and oligomers (e.g., oligopeptides and oligonucleotides), and synthetic organic compounds based on various core structures. In addition, various natural sources can provide compounds for screening, such as plant or animal extracts, and the like. A skilled artisan can readily recognize that there is no limit as to the structural nature of the agents of this disclosure. [0049] The term \"agonist\" as used herein refers to a compound or agent having the ability to initiate or enhance a biological function of a target protein or polypeptide, such as increasing the activity or expression of the target protein or polypeptide. Accordingly, the term \"agonist\" is defined in the context of the biological role of the target protein or polypeptide. While some agonists herein specifically interact with (e.g., bind to) the target, compounds and/or agents that initiate or enhance a biological activity of the target protein or polypeptide by interacting with other members of the signal transduction pathway of which the target polypeptide is a member are also specifically included within this definition. [0050] The terms \"antagonist\" and \"inhibitor\" are used interchangeably, and they refer to a compound or agent having the ability to inhibit a biological function of a target protein or polypeptide, such as by inhibiting the activity or expression of the target protein or polypeptide. Accordingly, the terms \"antagonist\" and \"inhibitor\" are defined in the context of the biological role of the target protein or polypeptide. While some antagonists herein specifically interact with (e.g., bind to) the target, compounds that inhibit a biological activity of the target protein or polypeptide by interacting with other members of the signal transduction pathway of which the target protein or polypeptide are also specifically included within this definition. Non-limiting examples of biological activity inhibited by an antagonist include those associated with the development, growth, or spread of a tumor, or an undesired immune response as manifested in autoimmune disease. [0051] An \"anti-cancer agent\", \"anti-tumor agent\" or \"chemotherapeutic agent\" refers to any agent useful in the treatment of a neoplastic condition. One class of anti-cancer agents comprises chemotherapeutic agents. \"Chemotherapy\" means the administration of one or more chemotherapeutic drugs and/or other agents to a cancer patient by various methods, including intravenous, oral, intramuscular, intraperitoneal, intravesical, subcutaneous, transdermal, or buccal administration, or inhalation, or in the form of a suppository. [0052] The term \"cell proliferation\" refers to a phenomenon by which the cell number has changed as a result of division. This term also encompasses cell growth by which the cell morphology has changed (e.g., increased in size) consistent with a proliferative signal. [0053] The term \"co-administration,\" \"administered in combination with,\" and their grammatical equivalents, as used herein, encompass administration of two or more agents to subject so that both agents and/or their metabolites are present in the subject at the same time. Co-administration includes simultaneous administration in separate compositions, administration at different times in separate compositions, or administration in a composition in which both agents are present. [0054] The term \"effective amount\" or \"therapeutically effective amount\" refers to that amount of a compound or pharmaceutical composition described herein that is sufficient to effect the intended application including, but not limited to, disease treatment, as illustrated below. The therapeutically effective amount can vary depending upon the intended application (in vitro or in vivo), or the subject and disease condition being treated, e.g., the weight and age of the subject, the severity of the disease condition, the manner of administration and the like, which can readily be determined by one of ordinary skill in the art. The term also applies to a dose that will induce a particular response in target cells, e.g., reduction of platelet adhesion and/or cell migration. The specific dose will vary depending on, for example, the particular compounds chosen, the dosing regimen to be followed, whether it is administered in combination with other agents, timing of administration, the tissue to which it is administered, and the physical delivery system in which it is carried. [0055] As used herein, the terms \"treatment\", \"treating\", \"palliating\" and \"ameliorating\" are used interchangeably herein. These terms refer to an approach for obtaining beneficial or desired results including, but not limited to, therapeutic benefit. By therapeutic benefit is meant eradication or amelioration of the underlying disorder being treated. Also, a therapeutic benefit is achieved with the eradication or amelioration of one or more of the physiological symptoms associated with the underlying disorder such that an improvement is observed in the patient, notwithstanding that the patient can still be afflicted with the underlying disorder. [0056] As used herein, the terms \"prevention\" and \"preventing\" are used herein to refer to an approach for obtaining beneficial or desired results including, but not limited, to prophylactic benefit. For prophylactic benefit, the pharmaceutical compositions can be administered to a patient at risk of developing a particular disease, or to a patient reporting one or more of the physiological symptoms of a disease, even though a diagnosis of this disease may not have been made. [0057] A \"therapeutic effect,\" as that term is used herein, encompasses a therapeutic benefit and/or a prophylactic benefit as described above. A prophylactic effect includes delaying or eliminating the appearance of a disease or condition, delaying or eliminating the onset of symptoms of a disease or condition, slowing, halting, or reversing the progression of a disease or condition, or any combination thereof. [0058] \"Signal transduction\" is a process during which stimulatory or inhibitory signals are transmitted into and within a cell to elicit an intracellular response. A \"modulator\" of a signal transduction pathway refers to a compound which modulates the activity of one or more cellular proteins mapped to the same specific signal transduction pathway. A modulator can augment (agonist) or suppress (antagonist) the activity of a signaling molecule. [0059] The term \"selective inhibition\" or \"selectively inhibit\" as applied to a biologically active agent refers to the agent's ability to selectively reduce the target signaling activity as compared to off- target signaling activity, via direct or indirect interaction with the target. For example, a compound that selectively inhibits one isoform of PI3K over another isoform of PI3K has an activity of at least greater than about IX against a first isoform relative to the compound's activity against the second isoform (e.g., at least about 2X, 3X, 5X, 10X, 20X, 50X, 100X, 200X, 500X, or 1000X). In certain embodiments, these terms refer to a compound described herein that selectively inhibits the delta isoform over the alpha or beta isoform. By way of non-limiting example, the ratio of selectivity can be greater than a factor of about 1, greater than a factor of about 2, greater than a factor of about 3, greater than a factor of about 5, greater than a factor of about 10, greater than a factor of about 50, greater than a factor of about 100, greater than a factor of about 200, greater than a factor of about 400, greater than a factor of about 600, greater than a factor of about 800, greater than a factor of about 1000, greater than a factor of about 1500, greater than a factor of about 2000, greater than a factor of about 5000, greater than a factor of about 10,000, or greater than a factor of about 20,000, where selectivity can be measured by IC 50 e.g., in vitro or in vivo assays such as those described in Examples 222, 224, 225, 226, 247, 248, etc. In certain embodiments, the PI3K delta isoform IC 50 activity of a compound provided herein can be less than about 1000 nM, less than about 500 nM, less than about 400 nM , less than about 300 nM, less than about 200 nM, less than about 100 nM, less than about 75 nM, less than about 50 nM, less than about 25 nM, less than about 20 nM, less than about 15 nM, less than about 10 nM, less than about 5 nM, or less than about 1 nM. [0060] \"Radiation therapy\" means exposing a patient, using routine methods and compositions known to the practitioner, to radiation emitters such as, but not limited to, alpha-particle emitting radionuclides (e.g., actinium and thorium radionuclides), low linear energy transfer (LET) radiation emitters (e.g., beta emitters), conversion electron emitters (e.g., strontium-89 and samarium-153-EDTMP), or high-energy radiation, including without limitation x-rays, gamma rays, and neutrons. [0061] \"Subject\" to which administration is contemplated includes, but is not limited to, humans (e.g., a male or female of any age group, e.g., a pediatric subject (e.g., infant, child, adolescent) or adult subject (e.g., young adult, middle-aged adult or senior adult)) and/or other primates (e.g. , cynomolgus monkeys, rhesus monkeys); mammals, including commercially relevant mammals such as cattle, pigs, horses, sheep, goats, cats, and/or dogs; and/or birds, including commercially relevant birds such as chickens, ducks, geese, quail, and/or turkeys. [0062] The term \"in vivo\" refers to an event that takes place in a subject's body. [0063] The term \"in vitro\" refers to an event that takes places outside of a subject's body. For example, an in vitro assay encompasses any assay conducted outside of a subject In vitro assays encompass cell-based assays in which cells, alive or dead, are employed. In vitro assays also encompass a cell-free assay in which no intact cells are employed. [0064] As used herein, \"pharmaceutically acceptable esters\" include, but are not limited to, alkyl, alkenyl, alkynyl, aryl, aralkyl, and cycloalkyl esters of acidic groups, including, but not limited to, carboxylic acids, phosphoric acids, phosphinic acids, sulfonic acids, sulfuric acids, and boronic acids. [0065] As used herein, \"pharmaceutically acceptable enol ethers\" include, but are not limited to, derivatives of formula -C=C(OR) where R can be selected from alkyl, alkenyl, alkynyl, aryl, aralkyl, and cycloalkyl. Pharmaceutically acceptable enol esters include, but are not limited to, derivatives of formula - C=C(OC(0)R) where R can be selected from hydrogen, alkyl, alkenyl, alkynyl, aryl, aralkyl, and cycloalkyl. [0066] As used herein, a \"pharmaceutically acceptable form\" of a disclosed compound includes, but is not limited to, pharmaceutically acceptable salts, hydrates, solvates, isomers, prodrugs, polymorphs, and isotopically labeled derivatives of disclosed compounds. In one embodiment, a \"pharmaceutically acceptable form\" includes, but is not limited to, pharmaceutically acceptable salts, isomers, prodrugs polymorphs, and isotopically labeled derivatives of disclosed compounds. [0067] In certain embodiments, the pharmaceutically acceptable form is a pharmaceutically acceptable salt. As used herein, the term \"pharmaceutically acceptable salt\" refers to those salts which are, within the scope of sound medical judgment, suitable for use in contact with the tissues of subjects without undue toxicity, irritation, allergic response and the like, and are commensurate with a reasonable benefit/risk ratio. Pharmaceutically acceptable salts are well known in the art. For example, Berge et al. describes pharmaceutically acceptable salts in detail in J. Pharmaceutical Sciences (1977) 66: 1-19. Pharmaceutically acceptable salts of the compounds provided herein include those derived from suitable inorganic and organic acids and bases. Examples of pharmaceutically acceptable, nontoxic acid addition salts are salts of an amino group formed with inorganic acids such as hydrochloric acid, hydrobromic acid, phosphoric acid, sulfuric acid and perchloric acid or with organic acids such as acetic acid, oxalic acid, maleic acid, tartaric acid, citric acid, succinic acid or malonic acid or by using other methods used in the art such as ion exchange. Other pharmaceutically acceptable salts include adipate, alginate, ascorbate, aspartate, benzenesulfonate, besylate, benzoate, bisulfate, borate, butyrate, camphorate, camphorsulfonate, citrate, cyclopentanepropionate, digluconate, dodecylsulfate, ethanesulfonate, formate, fumarate, glucoheptonate, glycerophosphate, gluconate, hemisulfate, heptanoate, hexanoate, hydroiodide, 2-hydroxy-ethanesulfonate, lactobionate, lactate, laurate, lauryl sulfate, malate, maleate, malonate, methanesulfonate, 2-naphthalenesulfonate, nicotinate, nitrate, oleate, oxalate, palmitate, pamoate, pectinate, persulfate, 3-phenylpropionate, phosphate, picrate, pivalate, propionate, stearate, succinate, sulfate, tartrate, thiocyanate, p-toluenesulfonate, undecanoate, valerate salts, and the like. In some embodiments, organic acids from which salts can be derived include, for example, acetic acid, propionic acid, glycolic acid, pyruvic acid, oxalic acid, maleic acid, malonic acid, succinic acid, fumaric acid, tartaric acid, citric acid, benzoic acid, cinnamic acid, mandelic acid, methanesulfonic acid, ethanesulfonic acid, p-toluenesulfonic acid, salicylic acid, and the like. [0068] Pharmaceutically acceptable salts derived from appropriate bases include alkali metal, alkaline earth metal, ammonium and salts. Representative alkali or alkaline earth metal salts include sodium, lithium, potassium, calcium, magnesium, iron, zinc, copper, manganese, aluminum, and the like. Further pharmaceutically acceptable salts include, when appropriate, nontoxic ammonium, quaternary ammonium, and amine cations formed using counterions such as halide, hydroxide, carboxylate, sulfate, phosphate, nitrate, lower alkyl sulfonate, and aryl sulfonate. Organic bases from which salts can be derived include, for example, primary, secondary, and tertiary amines, substituted amines including naturally occurring substituted amines, cyclic amines, basic ion exchange resins, and the like, such as isopropylamine, trimethylamine, diethylamine, triethylamine, tripropylamine, and ethanolamine. In some embodiments, the pharmaceutically acceptable base addition salt is chosen from ammonium, potassium, sodium, calcium, and magnesium salts. [0069] In certain embodiments, the pharmaceutically acceptable form is a solvate (e.g., a hydrate). As used herein, the term \"solvate\" refers to compounds that further include a stoichiometric or non-stoichiometric amount of solvent bound by non-covalent intermolecular forces. The solvate can be of a disclosed compound or a pharmaceutically acceptable salt thereof. Where the solvent is water, the solvate is a \"hydrate\". Pharmaceutically acceptable solvates and hydrates are complexes that, for example, can include 1 to about 100, or 1 to about 10, or one to about 2, about 3 or about 4, solvent or water molecules. It will be understood that the term \"compound\" as used herein encompasses the compound and solvates of the compound, as well as mixtures thereof. [0070] In certain embodiments, the pharmaceutically acceptable form is a prodrug. As used herein, the term \"prodrug\" refers to compounds that are transformed in vivo to yield a disclosed compound or a pharmaceutically acceptable form of the compound. A prodrug can be inactive when administered to a subject, but is converted in vivo to an active compound, for example, by hydrolysis (e.g., hydrolysis in blood). In certain cases, a prodrug has improved physical and/or delivery properties over the parent compound. Prodrugs are typically designed to enhance pharmaceutically and/or pharmacokinetically based properties associated with the parent compound. The prodrug compound often offers advantages of solubility, tissue compatibility or delayed release in a mammalian organism (see, e.g., Bundgard, H., Design of Prodrugs (1985), pp. 7-9, 21-24 (Elsevier, Amsterdam). A discussion of prodrugs is provided in Higuchi, T., et al., \"Pro-drugs as Novel Delivery Systems,\" A. C.S. Symposium Series, Vol. 14, and in Bioreversible Carriers in Drug Design, ed. Edward B. Roche, American Pharmaceutical Association and Pergamon Press, 1987, both of which are incorporated in full by reference herein. Exemplary advantages of a prodrug can include, but are not limited to, its physical properties, such as enhanced water solubility for parenteral administration at physiological pH compared to the parent compound, or it enhances absorption from the digestive tract, or it can enhance drug stability for long-term storage. [0071] The term \"prodrug\" is also meant to include any covalently bonded carriers, which release the active compound in vivo when such prodrug is administered to a subject. Prodrugs of an active compound, as described herein, can be prepared by modifying functional groups present in the active compound in such a way that the modifications are cleaved, either in routine manipulation or in vivo, to the parent active compound. Prodrugs include compounds wherein a hydroxy, amino or mercapto group is bonded to any group that, when the prodrug of the active compound is administered to a subject, cleaves to form a free hydroxy, free amino or free mercapto group, respectively. Examples of prodrugs include, but are not limited to, acetate, formate and benzoate derivatives of an alcohol or acetamide, formamide and benzamide derivatives of an amine functional group in the active compound and the like. Other examples of prodrugs include compounds that comprise -NO, -N0 2 , -ONO, or -ON0 2 moieties. Prodrugs can typically be prepared using well-known methods, such as those described in Burger's Medicinal Chemistry and Drug Discovery, 172-178, 949-982 (Manfred E. Wolff ed., 5th ed., 1995), and Design of Prodrugs (H. Bundgaard ed., Elsevier, New York, 1985). [0072] For example, if a disclosed compound or a pharmaceutically acceptable form of the compound contains a carboxylic acid functional group, a prodrug can comprise a pharmaceutically acceptable ester formed by the replacement of the hydrogen atom of the acid group with a group such as (Ci-C 8 )alkyl, (C 2 - Ci 2 )alkanoyloxymethyl, l-(alkanoyloxy)ethyl having from 4 to 9 carbon atoms, 1 -methyl- l-(alkanoyloxy)-ethyl having from 5 to 10 carbon atoms, alkoxycarbonyloxymethyl having from 3 to 6 carbon atoms, 1- (alkoxycarbonyloxy)ethyl having from 4 to 7 carbon atoms, 1 -methyl- 1 -(alkoxycarbonyloxy)ethyl having from 5 to 8 carbon atoms, N-(alkoxycarbonyl)aminomethyl having from 3 to 9 carbon atoms, 1-(N- (alkoxycarbonyl)amino)ethyl having from 4 to 10 carbon atoms, 3-phthalidyl, 4-crotonolactonyl, gamma- butyrolacton-4-yl, di-N,N-(Ci-C 2 )alkylamino(C 2 -C3)alkyl (such as β-dimethylaminoethyl), carbamoyl-(Ci- C 2 )alkyl, N,N-di(Ci-C 2 )alkylcarbamoyl-(Ci-C 2 )alkyl and piperidino-, pyrrolidino- or morpholino(C 2 -C3)alkyl. [0073] Similarly, if a disclosed compound or a pharmaceutically acceptable form of the compound contains an alcohol functional group, a prodrug can be formed by the replacement of the hydrogen atom of the alcohol group with a group such as (Ci-C 6 )alkanoyloxymethyl, l-((Ci-C 6 )alkanoyloxy)ethyl, 1 -methyl- 1- ((C ! -C 6 )alkanoyloxy)ethyl (Q-C^alkoxycarbonyloxymethyl, N-(C 1 -C 6 )alkoxycarbonylaminomethyl, succinoyl, (Ci-C6)alkanoyl, a-amino(Ci-C4)alkanoyl, arylacyl and a-aminoacyl, or α-aminoacyl-a-aminoacyl, where each a- aminoacyl group is independently selected from naturally occurring L-amino acids, P(0)(OH) 2 , -P(0)(0(Ci-C6)alkyl) 2 , and glycosyl (the radical resulting from the removal of a hydroxyl group of the hemiacetal form of a carbohydrate). [0074] If a disclosed compound or a pharmaceutically acceptable form of the compound incorporates an amine functional group, a prodrug can be formed by the replacement of a hydrogen atom in the amine group with a group such as R-carbonyl, RO-carbonyl, NRR'-carbonyl where R and R' are each independently (Ci-Cio)alkyl, (C 3 - C 7 )cycloalkyl, benzyl, a natural a-aminoacyl or natural a-aminoacyl-natural a-aminoacyl, -C(OH)C(0)OY 1 wherein Y 1 is H, (C C 6 )alkyl or benzyl, -C(OY 2 )Y 3 wherein Y 2 is (C C 4 ) alkyl and Y 3 is (C C 6 )alkyl, carboxy(C C 6 )alkyl, amino(Ci-C4)alkyl or mono-N- or di-N,N-(Ci-C6)alkylaminoalkyl, -C(Y 4 )Y 5 wherein Y 4 is H or methyl and Y 5 is mono-N- or di-N,N-(Ci-C6)alkylamino, mo holino, piperidin- 1 -yl or pyrrolidin-l-yl. [0075] In certain embodiments, the pharmaceutically acceptable form is an isomer. \"Isomers\" are different compounds that have the same molecular formula. \"Atropisomers\" are stereoisomers from hindered rotation about single bonds and can be resolved or isolated by methods known to those skilled in the art. For example, certain substituents of a compound of Formula (I) provided herein with ortho or meta substituted phenyl may form atropisomers, where they may be separated and isolated. [0076] \"Stereoisomers\" are isomers that differ only in the way the atoms are arranged in space. As used herein, the term \"isomer\" includes any and all geometric isomers and stereoisomers. For example, \"isomers\" include geometric double bond cis- and iraws-isomers, also termed E— and Z isomers; R- and iS-enantiomers; diastereomers, (4 and filtered. The filtrate is concentrated in vacuo and the residue is dissolved in MeOH (e.g., 1200 mL) at RT. To this solution, D-(-)-tartaric acid (0.8 eq, e.g., 21 g, 140 mmol) is added in one portion at RT. After stirring at RT for 30 min, a white solid precipitates and the mixture is slurried at RT for 10 h. The solid is collected by filtration and rinsed with MeOH (e.g., 3 x 50 mL). The collected solid is suspended in water (e.g., 500 mL) and then neutralized with concentrated ammonium hydroxide solution at RT to adjust the pH to 9-10. The mixture is extracted with DCM (e.g., 3 x 200 mL). The combined organic layers are washed with brine, dried over MgS0 4 and filtered. The filtrate is concentrated in vacuo to afford the (iS)-3-(l-aminoethyl)-isoquinolin- l(2H)-ones (A-3). [00431] Alternatively, the core can be synthesized as follows: i-PrMgCI B-3 B-4 B-5 Y = F, CI, Br, I, OTf B = phenyl, substituted phenyl, pyridinyl, or substituted pyridinyl Method B: [00432] An o-methylbenzoic acid (B-l) (1 eq, e.g., 46.9 mmol) in a flame-dried round bottom flask under nitrogen is dissolved in THF (e.g., 50 mL). The resulting homogeneous yellow solution is cooled to -25 °C and n- hexyllithium (4.3 eq, e.g., 202 mmol) (2.3 M in hexanes) is slowly added, after which the solution becomes dark red and is stirred at -20 °C for 20 min. [00433] (S)-Tert-butyl l-(methoxy(methyl)amino)-l-oxopropan-2-ylcarbamate (1.3 eq, e.g., 61.0 mmol) is charged into a second dry round bottom flask under N 2 and suspended in 70 mL of dry THF and cooled to -10 °C. Isopropyl magnesium chloride (2 M, 2.7 eq, e.g., 127 mmol) is slowly added resulting in a clear yellow solution. This solution is then slowly canulated dropwise into the first round bottom flask. After addition is complete, the dark solution is slowly warmed to RT and stirred at RT for 2 h. The reaction mixture is then recooled to -10 °C and quickly canulated into another flask fitted with 15 mL of ethyl acetate and 10 mL of isobutyric acid at -10°C under N 2 . During this time the mixture goes from orange and cloudy to clear and homogeneous. After addition, the mixture is stirred for 5 min after which water (e.g., 10 mL) is rapidly added and it is stirred vigorously for 10 min at RT. [00434] The mixture is then transferred to a separation funnel, and water (e.g., 200 mL) is added to dissolve salts (pH ~ 9). The water layer is extracted with EtOAc (e.g., 3 x 400 mL). The aqueous layer is then acidified with HCl (2 M) to pH 3, and then extracted with EtOAc (e.g., 3 x 500 mL), dried over sodium sulfate and concentrated to provide crude material which is filtered under vacuum through a pad of silica gel using a MeOH/DCM (gradient of 2-10% MeOH) to provide the acid B-2 after concentration. [00435] A 50 mL round bottom flask with a stir bar is filled with benzoic acid B-2 (e.g., 14.63 mmol) in acetic anhydride (e.g., 10 mL) and then stirred at 70 °C for 2.5 hours until complete conversion to the product is indicated by LC/MS. The acetic anhydride is evaporated under reduced pressure and the crude residue is purified with combiflash (gradient of EtOAc/hexanes) to give the lactone B-3. [00436] A 50 mL dry round bottom flask with a stir bar is filled with amine B-NH 2 (5.1 eq, e.g., 1.54 mmol) in 2 mL of DCM after which trimethylaluminum (5.1 eq, e.g., 1.54 mmol) is added to the solution and stirred for 15 min. A solution of lactone H-3 (1.0 eq, e.g., 0.31 mmol) in 2 mL of DCM is then added. The mixture is then stirred at RT for 3 h until LC/MS analysis showed complete formation of the desired product. The reaction mixture is quenched with 10 mL of Rochelle's salt and stirred for 2 h. The mixture is then diluted with DCM, washed with brine, dried with over sodium sulfate and evaporated to give a yellow sticky liquid B-4 which is used directly in next step. [00437] To the amide B-4 (e.g., 0.31 mmol) in 5 mL of isopropanol was added 3 mL of concentrated HCl. The mixture is then heated in an oil bath at 65 °C for 3 h until LC/MS shows no remaining starting material. The flask is then removed from heat and the solvents are evaporated under reduced pressure to provide a yellow solid B- 5 which is used directly in subsequent transformations. 1-13 Method C: [00438] To a solution of 2-chloro-6-methylbenzoic acid 1-7 (1.0 eq, e.g., 50 g, 294 mmol) in cone. H 2 SO 4 (e.g., 500 mL) at 0 °C, fuming HNO 3 (1.1 eq, e.g., 20.4 g, 324 mmol) was added slowly. The resulting mixture was stirred at 0 °C for 5 min and then stirred at RT for 2 h. The reaction mixture was poured into ice-water (e.g., 800 mL) and extracted with ethyl acetate (e.g., 3 x 500 mL). The combined organic layers were washed with brine, dried over Na 2 S0 4 and filtered. The filtrate was concentrated in vacuo to afford the product as a mixture of two regio- isomers, 6-chloro-2-methyl-3-nitrobenzoic acid 1-8 and 6-chloro-2-methyl-5-nitrobenzoic acid 1-8'. The mixture was used directly in the next step. [00439] To a stirred solution of above obtained regio-isomer mixture of 6-chloro-2-methyl-3-nitrobenzoic acid 8 and 6-chloro-2-methyl-5-nitrobenzoic acid 1-8' (1.0 eq, e.g., 61.8 g, 287 mmol) and DMF (catalytic amount) in DCM (e.g., 500 mL) at RT, oxalyl chloride (2.0 eq, e.g., 49 mL, 574 mmol) was added slowly (e.g., over 5 min). The resulting mixture was stirred at RT for 2 h and then concentrated in vacuo. The residue was dissolved in DCM (150 mL) to form solution A. [00440] To a mixture of aniline (1.2 eq, e.g., 32 g, 344 mmol) and triethylamine (3.0 eq, e.g., 87.5 g, 861 mmol) in DCM (e.g., 400 mL) at RT, solution A was added dropwise. The resulting mixture was stirred for 15 min and then quenched with water (500 mL). The organic layer was separated and the aqueous layer was extracted with DCM (e.g., 3 x 500 mL). The combined organic layers were washed with brine, dried over Na 2 S0 4 and filtered. The filtrate was concentrated in vacuo to afford the product as a mixture of two regio-isomers, 6-chloro-2-methyl-3- nitro-N-phenylbenzamide 1-9 and 2-chloro-6-methyl-3-nitro-N-phenylbenzamide 1-9'. The mixture was used directly in the next step. [00441] To a stirred mixture of 6-chloro-2-methyl-3-nitro-N-phenylbenzamide 9 and 2-chloro-6-methyl-3- nitro-N-phenylbenzamide 1-9' (1.0 eq, e.g., 33.6.8 g, 116 mmol) in EtOH (e.g., 400 mL), SnCl 2 2H 2 0 (4.0 eq, e.g., 105 g, 464 mmol) was added and the resulting mixture was stirred at reflux for 3 h. The reaction mixture was allowed to cool and concentrated in vacuo. The residue was poured into water (e.g., 500 mL) and the mixture was extracted with ethyl acetate (e.g., 5 x 500 mL). The combined organic layers were washed with brine, dried over Na 2 S0 4 and filtered. The filtrate was concentrated in vacuo. The residue was purified by flash column chromatography on silica gel (2-20% ethyl acetate-petroleum ether) to afford the regio-isomer, 3-amino-6-chloro-2- methyl-N-phenylbenzamide 1-10. The remaining mixture of 3-amino-6-chloro-2-methyl-N-phenylbenzamide 1-10 and 5-amino-6-chloro-2-methyl-N-phenylbenzamide 1-10' was collected separately. Compound 1-10' was obtained by further column chromatography purification. [00442] To a stirred mixture of 1-10' in fluoroboric acid at 0 °C, a solution of sodium nitrate in H 2 0 is added dropwise over 30 min while keeping the reaction temperature between 0 °C and 5 °C. The resulting mixture is stirred at RT for 16 h. The precipitate is collected by filtration, rinsed with cold water, and dried in vacuo to afford 1-11, which is used directly in the next step. [00443] The intermediate product 1-11 is heated to 120 °C and the temperature is maintained between 120 °C and 130 °C for 1 h. The mixture was cooled to 50 °C and poured into ice -water. The resulting mixture is extracted with ethyl acetate. The combined organic layers are washed with brine, dried over Na 2 S0 4 and filtered. The filtrate is concentrated in vacuo and the residue is purified by flash column chromatography on silica gel (2-20% ethyl acetate-hexanes) to afford 1-12. [00444] Compound 1-12 can be converted to 1-13 using Method A or B. F-3 F-4 F-5 Method F: [00445] To a stirred mixture of nitrobenzoic acid (F-1) (1.0 eq, e.g., 1.0 mol) and DMF (e.g., 2.0 mL) in toluene (e.g., 800 mL), thionyl chloride (4.0 eq, e.g., 292 mL, 1.0 mol) is added dropwise (e.g., over 15 min) and the resulting mixture is stirred at reflux for 1.5 h. The mixture is allowed to cool to RT and then concentrated in vacuo. The residue is dissolved in DCM (e.g., 100 mL) to form solution A, which is used directly in the next step. [00446] To a stirred mixture of a given amine R 2 -NH 2 (1.1 eq, e.g., 102.4 g, 1.1 mol) and triethylamine (2.0 eq, e.g., 280 mL, 2.0 mol) in DCM (e.g., 700 mL), solution A is added dropwise while keeping the reaction temperature below 10 °C. The resulting mixture is allowed to warm to RT and then stirred at RT overnight. The reaction mixture is diluted with ice-water (e.g., 1.0 L) and stirred for 15 min. The precipitate is collected by filtration, rinsed with isopropyl ether (e.g., 3 x 100 mL) and petroleum ether (e.g., 3 x 100 mL), and then dried in vacuo to afford product amide (F-2). [00447] A mixture of nitro-benzamide (F-2) (1.0 eq, e.g., 20.0 mmol) and DMF (cat.) in toluene (e.g., 60 mL) at RT, thionyl chloride (8.2 eq, e.g., 12 mL , 164 mmol) is added dropwise (e.g., over 5 min) and the resulting mixture is stirred at reflux for 2 h. The mixture is allowed to cool to RT and then concentrated in vacuo. The residue is dissolved in DCM (e.g., 10 mL) to form solution B, which is used directly in the next step. [00448] To a stirred mixture of A^-(feri-butoxycarbonyl)-L-alanine (0.8 eq, e.g., 16.0 mmol) and N,N- diisopropylethylamine (1.5 eq, e.g., 4.0 g, 31.0 mol) in DCM (e.g., 20 mL), solution B is added dropwise while keeping the reaction temperature between 0-10 °C. The resulting mixture is stirred at this temperature for 1 h and then stirred at RT overnight. The reaction mixture is quenched with ice-water (e.g., 100 mL). The organic layer is separated and the aqueous layer is extracted with DCM (e.g., 2 x 80 mL). The combined organic layers are washed with brine, dried over Na 2 S0 4 and filtered. The filtrate is concentrated in vacuo and the residue is slurried in isopropyl ether (e.g., 100 mL) for 15 min. The solid is collected by filtration and dried in vacuo to afford product (F-3). [00449] To a suspension of zinc dust (10.0 eq, e.g., 7.2 g, 110 mmol) in glacial acetic acid (e.g., 40 mL) at 15 °C, a solution of (F-3) (1.0 eq, e.g., 11.0 mmol) in glacial acetic acid (e.g., 40 mL) is added and the resulting mixture is stirred at RT for 4 h. The mixture is poured into ice-water (e.g., 200 mL) and neutralized with saturated aqueous NaHC0 3 solution to adjust the pH to 8. The resulting mixture is extracted with DCM (e.g., 3 x 150 mL). The combined organic layers are washed with brine, dried over Na 2 S0 4 and filtered. The filtrate is concentrated in vacuo and the residue is purified by flash chromatography on silica gel (7% ethyl acetate-petroleum ether) to afford product (F-4). [00450] Compound (F-4) (1.0 eq, e.g., 0.5 mmol) is dissolved in hydrochloric methanol solution (2N, e.g., 20 mL) and the resulting mixture is stirred at RT for 2 h. The mixture is concentrated in vacuo. The residue is diluted with water (e.g., 30 mL) and then neutralized with saturated aqueous NaHC0 3 to adjust the pH to 8 while keeping the temperature below 5 °C. The resulting mixture is extracted with DCM (e.g., 3 x 30 mL). The combined organic layers are washed with brine, dried over Na 2 S0 4 and filtered. The filtrate is concentrated in vacuo and the residue is slurried in petroleum ether (e.g., 10 mL). The solid is collected by filtration and dried in vacuo to afford product (F-5). [00451] The quinazolinone (F-5) can be used to synthesize compounds described herein using, for example, Method D to couple the amine to W d groups. X-4 X-3 Method FF [00452] Alternatively, compounds with a quinazolinone core can be prepared according to the procedures in PCT publication no. WO2013082540. [00453] In Method FF, 2-Amino-6-chlorobenzoic acid (63 mmol, 1.0 equiv) is dissolved in acetonitrile (60 mL) in a 250 mL round bottomed-flask, placed under an atmosphere of Ar and heated to 50 °C. Pyridine (2.0 equiv) is added followed by dropwise the addition of a solution of triphosgene (0.34 equiv in 30 mL acetonitrile) while maintaining the internal temperature below 60 °C. The mixture is then stirred at 50 °C for 2h after which the solvent is removed under vacuum. The remaining residue is dispersed in 50 mL of water and filtered. The resulting solid is washed with a minimal amount of acetonitrile to remove discoloration and then dried to provide desired anhydride X-l. [00454] Anhydride X-l (25.5 mmol, 1.0 equiv) is suspended in dioxane (40 mL) under an atmosphere of Ar in a 200 mL round bottomed- flask. Aniline (1.0 equiv) is added dropwise. Heating is started at 40 °C and gradually increased to 100 °C. After 4h, the majority of starting material is consumed after which the reaction is allowed to cool. The solvent is then removed under vacuum to provide an oil which is redissolved in toluene followed by the addition of hexanes until the solvent appears close to partionning. The mixture is stirred for 14h after which a solid appeared in the flask. This solid is isolated via vacuum filtration and washed with hexanes to provide the desired amide X-2 in high yield. [00455] (iS)-2-((\"feri-Butoxycarbonyl)amino)propanoic acid (33.0 mmol, 2.0 equiv) is dissolved in dry tetrahydrofuran (70 mL) under an atmosphere of Ar after which A -methylmorpholine (2.2 equiv) is added dropwise. The mixture is then cooled to -17 °C in an acetone/dry ice bath after which a solution of isobutyl chloroformate (2.0 equiv in 10 mL of dry tetrahydrofuran) is added dropwise to the mixture followed by stirring for 30 min. A solution of amine X-2 (10 equiv in 10 mL of dry tetrahydrofuran) is then added. The dry ice bath is then removed and the mixture is stirred at RT for 90 min. It is then heated to 60 °C for another 2h after which it is allowed to cool. MTBE (150 mL) and water (150 mL) are then successively added with strong stirring. The phases are separated and the organic phase is washed with water (2 x 50 mL) and brine (50 mL) and dried over sodium sulfate. The solution is then concentrated under reduced pressure and the crude reside is purified using flash silica gel chromatography (gradient 5-30 ethyl acetate/hexanes) X-3 as the coupled product. [00456] Compound X-3 (4.9 mmol, 1.0 equiv) is then suspended in acetonitrile (100 mL). Triethylamine (48 equiv) is then added with stirring followed by the dropwise addition of chlorotrimethylsilane (15 equiv). The flask is then sealed and heated to 90 °C for 3d. The reaction is allowed to cool after which the solvent is removed under vacuum. The residue is then dissolved in ethyl acetate (120 mL) and successively washed with saturated sodium carbonate (1 x 100 mL), water (1 x 100 mL) and brine (1 x 100 mL). The organic layer is then dried over anhydrous sodium sulfate and concentrated under reduced pressure to provide cyclized product X-4. The product can either be used directly in subsequent reactions or purified using flash silica gel chromatography. General conditions for attachment of W d substituents: B = phenyl, substituted phenyl, pyridinyl, or substituted pyridinyl Z = CI, OTf Method D [00457] (S)-3-(l-Aminoethyl)-isoquinolin-l(2H)-one (A-3) (1.0 eq, e.g., 1 15 mmol), Cl-Wd or Wd- OTs (1.5 eq, e.g., 173 mmol) and triethylamine (3.0 eq, e.g., 344 mmol) are dissolved in n-BuOH (e.g., 350 mL) and the mixture is stirred at reflux for 16 h. The reaction mixture is cooled to RT and concentrated in vacuo. The residue is suspended in a mixture of H 2 0 (e.g., 200 mL) and ethyl acetate (e.g., 100 mL) and stirred at RT for 30 min. The solid is then collected by filtration, rinsed with ethyl acetate (e.g., 25 mL) and dried in vacuo to afford the product (G-l). The reaction can occur under other conditions known in the art that are suitable for S AT displacement reaction. In one embodiment, the reaction solvent is NMP. Example 1: Preparation of Compound Is [00458] Compound A (1.50 g, 6.54 mmol, 1 eq.) was dissolved in anhydrous THF (10 mL), cooled to 0°C and stirred for 10 min. The flask was charged with a 2.2 M solution of n-hexyl lithium in hexane (6.54 mL, 14.39 mmol, 2.2 eq.), keeping the temperature under 5°C. In another flask, compound B (1.93 g, 7.85 mmol, 1.2 eq.) was dissolved in anhydrous THF (10 mL), cooled to 0°C and stirred for 10 min. The flask was charged with a 2 M solution of isopropyl magnesium chloride in THF (4.91 mL, 9.81 mmol, 1.5 eq.), keeping the temperature under 5°C. Both reactions were stirred for 15 min. The content of the second flask was charged into the first flask, keeping the temperature under 5°C. The reaction was allowed to warm at room temperature and was stirred for 2 hr. The reaction was diluted with ethyl acetate (20 mL) and was charged with a solution of citric acid (6.29 g, 32.70 mmol, 5 eq.) in water (20 mL). The organic layer was separated, washed with brine, dried over anhydrous sodium sulfate and purified on silica gel column with ethyl acetate and hexanes to afford the desired compound C. ESI-MS m/z: 415.2 [M+H] + . [00459] Compound C (2.30 g, 5.55 mmol, 1 eq.) was dissolved in ethyl acetate (40 mL) at room temperature. The solution was charged with methanesulfonic acid (1.44 mL, 22.20 mmol, 4 eq.) and was stirred at room temperature for 20 hr. The solution was heated at 50°C for 5 hr and cooled at 0°C. A 0.4% solution of ammonium hydroxide in water (47.72 mL, 55.50 mmol, 10 eq.) was added dropwise onto the reaction mixture, keeping the temperature under 10°C. The organic layer was separated, washed with brine, dried over anhydrous sodium sulfate and evaporated to yield the desired compound B. ESI-MS m/z: 297.1 [M+H] + . [00460] Compound D (0.20 g, 0.69 mmol, 1 eq.), compound E (0.32 g, 1.35 mmol, 2 eq.) and triethylamine (0.24 mL, 1.71 mmol, 2.5 eq.) were dissolved in isopropyl alcohol (3 mL). The reaction was stirred at 80°C for 30 hr and was allowed to cool at room temperature. The solid was filtered, washed with isopropyl alcohol and dried to afford the desired compound F. ESI-MS m/z: 499.3 [M+H] + . [00461] Compound F (0.20 g, 0.40 mmol, 1 eq.), was suspended in ethanol (3 mL) and charged with a 2 M solution of hydrogen chloride in water (0.60 mL, 1.20 mmol, 3 eq.). The reaction was stirred at 30°C for 3 hr and was allowed to cool at room temperature. A 5% solution of ammonium hydroxide in water (1.16 mL, 1.61 mmol, 4 eq.) was added dropwise onto the reaction. Solvents were removed under reduced pressure and the residue was partitioned between water and ethyl acetate, dried over anhydrous sodium sulfate and evaporated to yield the desired product Is. ESI-MS m/z: 415.2 [M+H] + . Example 2: Preparation of Compound 96s 1-15 Compound 96s [00462] Compound 96s can be prepared starting with 1-15 according to Method D. ESI-MS m/z: 435.2 [M+H]+. Biological Activity Assessment Table 7. In Vitro IC 50 data The data in Table 7 are coded as follows. A = 1 to <10 nM B = 10 to <100 nM C = 100 to <3500 nM D = 3500 to <10000 nM Example 222: PI3-Kinase HTRF™ Assay [00463] A PI3 -Kinase HTRF® assay kit (cat No. 33-016) purchased from Millipore Corporation was used to screen compounds provided herein. This assay used specific, high affinity binding of the GRP1 pleckstrin homology (PH) domain to PIP3, the product of a Class 1A or IB PI3 Kinase acting on its physiological substrate PIP2. During the detection phase of the assay, a complex was generated between the GST-tagged PH domain and biotinylated short chain PIP3. The biotinylated PIP3 and the GST-tagged PH domain recruited fluorophores (Streptavidin-Allophycocyanin and Europium-labeled anti-GST respectively) to form the fluorescence resonance energy transfer (FRET) architecture, generating a stable time-resolved FRET signal. The FRET complex was disrupted in a competitive manner by non-biotinylated PIP3, a product formed in the PI3 Kinase assay. [00464] PI3 Kinase α, β, γ or δ activity was assayed using the PI3 Kinase HTRF® assay kit (catalogue No. 33-016) purchased from Millipore Corporation. Purified recombinant PI3Ka (catalogue No. 14-602-K), ΡΙ3Κβ (catalogue No. 14-603-K), ΡΙ3Κγ (catalogue No. 14-558-K), and PI3K6 (catalogue No. 14-604-K) were obtained from Millipore Corporation. Purified recombinant PI3K enzyme was used to catalyze the phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2 at 10 μΜ) to phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the presence of 10 μΜ ATP. The assay was carried out in 384-well format and detected using a Perkin Elmer EnVision Xcite Multilabel Reader. Emission ratios were converted into percent inhibitions and imported into GraphPad Prism software. The concentration necessary to achieve inhibition of enzyme activity by 50% (IC 50 ) was calculated using concentrations ranging from 20 μΜ to 0.1 nM (12-point curve). IC 50 values were determined using a nonlinear regression model available in GraphPad Prism 5. Example 223: Chemical Stability [00465] The chemical stability of one or more subject compounds is determined according to standard procedures known in the art. The following details an exemplary procedure for ascertaining chemical stability of a subject compound. The default buffer used for the chemical stability assay is phosphate-buffered saline (PBS) at pH 7.4; other suitable buffers can be used. A subject compound is added from a 100 μΜ stock solution to an aliquot of PBS (in duplicate) to give a final assay volume of 400 μΕ, containing 5 μΜ test compound and 1% DMSO (for half- life determination a total sample volume of 700 μΕ is prepared). Reactions are incubated, with shaking, for 24 hours at 37 °C; for half-life determination samples are incubated for 0, 2, 4, 6, and 24 hours. Reactions are stopped by adding immediately 100 μΕ of the incubation mixture to 100 μΕ of acetonitrile and vortexing for 5 minutes. The samples are then stored at -20 °C until analysis by HPLC -MS/MS. Where desired, a control compound or a reference compound such as chlorambucil (5 μΜ) is tested simultaneously with a subject compound of interest, as this compound is largely hydrolyzed over the course of 24 hours. Samples are analyzed via (RP)HPLC -MS/MS using selected reaction monitoring (SRM). The HPLC conditions consist of a binary LC pump with autosampler, a mixed-mode, CI 2, 2 x 20 mm column, and a gradient program. Peak areas corresponding to the analytes are recorded by HPLC-MS/MS. The ratio of the parent compound remaining after 24 hours relative to the amount remaining at time zero, expressed as percent, is reported as chemical stability. In case of half- life determination, the half-life is estimated from the slope of the initial linear range of the logarithmic curve of compound remaining (%) vs. time, assuming first order kinetics. Example 224: Expression and Inhibition Assays of ρ110α/ρ85α, ρ110β/ρ85α, ρ110δ/ρ85α, and ρΐΐθγ: [00466] Class I PI3-Ks can be either purchased (pi 10α/ρ85α, pi 10β/ρ85α, pi 10δ/ρ85α from Upstate, and pl lOy from Sigma) or expressed as previously described (Knight et al , 2004). IC 50 values are measured using either a standard TLC assay for lipid kinase activity (described below) or a high-throughput membrane capture assay. Kinase reactions are performed by preparing a reaction mixture containing kinase, inhibitor (2% DMSO final concentration), buffer (25 mM HEPES, pH 7.4, 10 mM MgCl 2 ), and freshly sonicated phosphatidylinositol (100 g/ml). Reactions are initiated by the addition of ATP containing 10 μθ of γ-32Ρ-ΑΤΡ to a final concentration of 10 or 100 μΜ and allowed to proceed for 5 minutes at room temperature. For TLC analysis, reactions are then terminated by the addition of 105 μΐ ^ IN HC1 followed by 160 μΐ ^ CHC^MeOH (1 : 1). The biphasic mixture is vortexed, briefly centrifuged, and the organic phase is transferred to a new tube using a gel loading pipette tip precoated with CHCI 3 . This extract is spotted on TLC plates and developed for 3-4 hours in a 65:35 solution of n- propanok lM acetic acid. The TLC plates are then dried, exposed to a phosphorimager screen (Storm, Amersham), and quantitated. For each compound, kinase activity is measured at 10-12 inhibitor concentrations representing two-fold dilutions from the highest concentration tested (typically, 200 μΜ). For compounds showing significant activity, IC 50 determinations are repeated two to four times, and the reported value is the average of these independent measurements. [00467] Other commercial kits or systems for assaying PI3-K activities are available. The commercially available kits or systems can be used to screen for inhibitors and/or agonists of PI3-Ks including, but not limited to, PI 3-Kinase α, β, δ, and γ. An exemplary system is PI 3-Kinase (human) HTRF™ Assay from Upstate. The assay can be carried out according to the procedures suggested by the manufacturer. Briefly, the assay is a time resolved FRET assay that indirectly measures PIP3 product formed by the activity of a PI3-K. The kinase reaction is performed in a microtiter plate (e.g., a 384 well microtiter plate). The total reaction volume is approximately 20 μΕ per well. In the first step, each well receives 2 μΕ of test compound in 20% dimethylsulphoxide resulting in a 2% DMSO final concentration. Next, approximately 14.5 μΕ of a kinase/PIP2 mixture (diluted in IX reaction buffer) is added per well for a final concentration of 0.25-0.3 μg/nlL kinase and 10 μΜ PIP2. The plate is sealed and incubated for 15 minutes at room temperature. To start the reaction, 3.5 μΕ of ATP (diluted in IX reaction buffer) is added per well for a final concentration of 10 μΜ ATP. The plate is sealed and incubated for 1 hour at room temperature. The reaction is stopped by adding 5 μΕ of Stop Solution per well and then 5 μΕ of Detection Mix is added per well. The plate is sealed, incubated for 1 hour at room temperature, and then read on an appropriate plate reader. Data is analyzed and IC 50 S are generated using GraphPad Prism 5. Example 225: B Cell Activation and Proliferation Assay [00468] The ability of one or more subject compounds to inhibit B cell activation and proliferation is determined according to standard procedures known in the art. For example, an in vitro cellular proliferation assay is established that measures the metabolic activity of live cells. The assay is performed in a 96 well microtiter plate using Alamar Blue reduction. Balb/c splenic B cells are purified over a Ficoll-Paque™ PLUS gradient followed by magnetic cell separation using a MACS B cell Isolation Kit (Miletenyi). Cells are plated in 90 μΐ ^ at 50,000 cells/well in B Cell Media (RPMI + 10% FBS + Penn/Strep + 50 μΜ bME + 5 mM HEPES). A compound provided herein is diluted in B Cell Media and added in a 10 μΕ volume. Plates are incubated for 30 min at 37 °C and 5% CO 2 (0.2% DMSO final concentration). A 50 μΕ B cell stimulation cocktail is then added containing either 10 μg/mL LPS or 5 μg/mL F(ab')2 Donkey anti-mouse IgM plus 2 ng/niL recombinant mouse IL4 in B Cell Media. Plates are incubated for 72 hours at 37 °C and 5% CO 2 . A volume of 15 μΕ of Alamar Blue reagent is added to each well and plates are incubated for 5 hours at 37 °C and 5% CO 2 . Alamar Blue fluoresce is read at 560Ex/590Em, and IC 50 or EC 50 values are calculated using GraphPad Prism 5. Example 226: Tumor Cell Line Proliferation Assay [00469] The ability of one or more subject compounds to inhibit tumor cell line proliferation can be determined according to standard procedures known in the art. For instance, an in vitro cellular proliferation assay can be performed to measure the metabolic activity of live cells. The assay is performed in a 96-well microtiter plate using Alamar Blue reduction. Human tumor cell lines are obtained from ATCC (e.g., MCF7, U-87 MG, MDA-MB-468, PC-3), grown to confluency in T75 flasks, trypsinized with 0.25% trypsin, washed one time with Tumor Cell Media (DMEM + 10%FBS), and plated in 90 xL at 5,000 cells/well in Tumor Cell Media. A compound provided herein is diluted in Tumor Cell Media and added in a 10 μΕ volume. Plates are incubated for 72 hours at 37 °C and 5% CO 2 . A volume of 10 μΕ of Alamar Blue reagent is added to each well and plates are incubated for 3 hours at 37 °C and 5% CO 2 . Alamar Blue fluoresce is read at 560Ex/590Em, and IC 50 values are calculated using GraphPad Prism 5. Example 227: Antitumor Activity in vivo [00470] The compounds described herein can be evaluated in a panel of human and murine tumor models. Paclitaxel-Refractory Tumor Models 1. Clinically-Derived Ovarian Carcinoma Model. [00471] This tumor model is established from a tumor biopsy of an ovarian cancer patient. Tumor biopsy is taken from the patient. The compounds described herein are administered to nude mice bearing staged tumors using an every 2 days x 5 schedule. 2. A2780Tax Human Ovarian Carcinoma Xenograft (Mutated Tubulin). [00472] A2780Tax is a paclitaxel-resistant human ovarian carcinoma model. It is derived from the sensitive parent A2780 line by co-incubation of cells with paclitaxel and verapamil, an MDR-reversal agent. Its resistance mechanism has been shown to be non-MDR related and is attributed to a mutation in the gene encoding the beta-tubulin protein. The compounds described herein can be administered to mice bearing staged tumors on an every 2 days x 5 schedule. 3. HCT116/VM46 Human Colon Carcinoma Xenograft (Multi-Drug Resistant). [00473] HCT116/VM46 is an MDR-resistant colon carcinoma developed from the sensitive HCT116 parent line. In vivo, grown in nude mice, HCT116/VM46 has consistently demonstrated high resistance to paclitaxel. The compounds described herein can be administered to mice bearing staged tumors on an every 2 days x 5 schedule. 4. M 5076 Murine Sarcoma Model [00474] M5076 is a mouse fibrosarcoma that is inherently refractory to paclitaxel in vivo. The compounds described herein can be administered to mice bearing staged tumors on an every 2 days x 5 schedule. One or more compounds as provided herein can be used in combination with other therapeutic agents in vivo in the multidrug resistant human colon carcinoma xenografts HCT/VM46 or any other model known in the art including those described herein. [00475] In one aspect, compounds provided herein can be evaluated in the following models according to methods known in the art. The dosage and schedule of administration can be varied depending on the model. The results can be evaluated with those of selective delta inhibitors, and combinations of delta and gamma inhibitors, and/or with antibodies that block specific inhibitory receptors. Pancreatic Models [00476] KPC model is a transgenic mouse model of pancreatic ductal adenocarcinoma (PDA), in which there is conditional expression of both mutant KrasG12D and p53R172H alleles in pancreatic cells. Tumors develop spontaneously in this mouse over a period of 3 -6 months, and can be used to study prophylactic, as well as therapeutic efficacy with novel agents. Cells from these KPC tumors can also be adoptively transferred into syngeneic C57BL/6 mice, creating a model with a shorter latency period and allowing large number of animals with tumors to be synchronously established. See e.g., Cancer Cell 7:468 (2005). [00477] Pan02 model: The murine pancreatic adenocarcinoma cell line Pan02 is a nonmetastatic tumor line, syngeneic to C57BL/6. It can be studied following s.c. injection into flank, or orthotopic ally following injection directly into the pancreas. See e.g., Cancer Res. 44: 717-726 (1984). Lung Models [00478] LLC Lewis Lung Adenocarcinoma model: LLC cells are derived from a spontaneous lung tumor from a C57BL/6 mouse and can be studied as a s.c. tumor when injected in the flank, or as an orthotopic tumor if injected i.v., following which it localizes to the lung. [00479] LLC cells have also been modified to express a peptide from ovalbumin (LL2-OVA cells). Use of these cells, following either s.c. or i.v. injection, allows the tracking of OVA-specific CD8+ lymphocyctes and measurement of effects of therapy on the adaptive immune response against the tumor. See e.g. , Science 330:827 (2010). Breast Model [00480] The 4T1 mammary carcinoma is a transplantable tumor cell line that grows in syngeneic BALB/c mice. It is highly tumorigenic and invasive and, unlike most tumor models, can spontaneously metastasize from the primary tumor in the mammary gland to multiple distant sites including lymph nodes, blood, liver, lung, brain, and bone. See e.g. , Current Protocols in Immunology Unit 20.2 (2000). Lymphoma Model [00481] EL4 is a C57BL/6 T thymoma and EG7 is an OVA-expressing subclone of EL4. The parental EL4 line has been modified to constitutively express luciferase, which allows non-invasive imaging of tumor growth throughout the animal using the Xenogen imaging platform. Melanoma Model [00482] B16 murine melanoma cells are syngeneic with C57BL/6 mice and can be studied after s.c. or i.v. injection. Placement at either site will result in metastases to lung and other organs. This model has been extensively studied in terms of the role that inhibitory receptors play in the anti-tumor immune response. See e.g., PNAS 107:4275 (2010). Example 228: Microsome Stability Assay [00483] The stability of one or more subject compounds is determined according to standard procedures known in the art. For example, stability of one or more subject compounds is established by an in vitro assay. For example, an in vitro microsome stability assay is established that measures stability of one or more subject compounds when reacting with mouse, rat or human microsomes from liver. The microsome reaction with compounds is performed in 1.5 mL Eppendorf tube. Each tube contains 0.1 μΕ of 10.0 mg/niL NADPH; 75 μΕ of 20.0 mg/niL mouse, rat or human liver microsome; 0.4 μΕ of 0.2 M phosphate buffer, and 425 μΕ of ddH 2 0. Negative control (without NADPH) tube contains 75 μΕ of 20.0 mg/niL mouse, rat or human liver microsome; 0.4 μΕ of 0.2 M phosphate buffer, and 525 μΕ of ddH 2 0. The reaction is started by adding 1.0 μΕ of 10.0 mM tested compound. The reaction tubes are incubated at 37 °C. 100 μΕ sample is collected into new Eppendorf tube containing 300 μΕ cold methanol at 0, 5, 10, 15, 30 and 60 minutes of reaction. Samples are centrifuged at 15,000 rpm to remove protein. Supernatant of centrifuged sample is transferred to new tube. Concentration of stable compound after reaction with microsome in the supernatant is measured by Liquid Chromatography/Mass Spectrometry (LC-MS). Example 229: Plasma Stability Assay [00484] The stability of one or more subject compounds in plasma is determined according to standard procedures known in the art. See, e.g., Rapid Commun. Mass Spectrom., 10: 1019-1026. The following procedure is an HPLC -MS/MS assay using human plasma; other species including monkey, dog, rat, and mouse are also available. Frozen, heparinized human plasma is thawed in a cold water bath and spun for 10 minutes at 2000 rpm at 4 °C prior to use. A subject compound is added from a 400 μΜ stock solution to an aliquot of pre-warmed plasma to give a final assay volume of 400 μΕ (or 800 μΕ for half- life determination), containing 5 μΜ test compound and 0.5 % DMSO. Reactions are incubated, with shaking, for 0 minutes and 60 minutes at 37 C, or for 0, 15, 30, 45 and 60 minutes at 37 C for half life determination. Reactions are stopped by transferring 50 μΕ of the incubation mixture to 200 μΕ of ice-cold acetonitrile and mixed by shaking for 5 minutes. The samples are centrifuged at 6000 x g for 15 minutes at 4 °C and 120 μΕ of supernatant removed into clean tubes. The samples are then evaporated to dryness and submitted for analysis by HPLC-MS/MS. [00485] In one embodiment, one or more control or reference compounds (5 μΜ) are tested simultaneously with the test compounds: one compound, propoxycaine, with low plasma stability and another compound, propantheline, with intermediate plasma stability. [00486] Samples are reconstituted in acetonitrile/methanol/water (1/1/2, v/v/v) and analyzed via (RP)HPLC-MS/MS using selected reaction monitoring (SRM). The HPLC conditions consist of a binary LC pump with autosampler, a mixed-mode, CI 2, 2 x 20 mm column, and a gradient program. Peak areas corresponding to the analytes are recorded by HPLC-MS/MS. The ratio of the parent compound remaining after 60 minutes relative to the amount remaining at time zero, expressed as percent, is reported as plasma stability. In case of half-life determination, the half-life is estimated from the slope of the initial linear range of the logarithmic curve of compound remaining (%) vs. time, assuming first order kinetics. Example 230: Kinase Signaling in Blood [00487] PI3K/Akt/mTOR signaling is measured in blood cells using the phosflow method {Methods Enzymol. (2007) 434: 131-54). This method is by nature a single cell assay so that cellular heterogeneity can be detected rather than population averages. This allows concurrent distinction of signaling states in different populations defined by other markers. Phosflow is also highly quantitative. To test the effects of one or more compounds provided herein, unfractionated splenocytes, or peripheral blood mononuclear cells are stimulated with anti-CD3 to initiate T-cell receptor signaling. The cells are then fixed and stained for surface markers and intracellular phosphoproteins. Inhibitors provided herein inhibit anti-CD3 mediated phosphorylation of Akt -S473 and S6, whereas rapamycin inhibits S6 phosphorylation and enhances Akt phosphorylation under the conditions tested. [00488] Similarly, aliquots of whole blood are incubated for 15 minutes with vehicle (e.g., 0.1% DMSO) or kinase inhibitors at various concentrations, before addition of stimuli to crosslink the T cell receptor (TCR) (anti- CD3 with secondary antibody) or the B cell receptor (BCR) using anti-kappa light chain antibody (Fab'2 fragments). After approximately 5 and 15 minutes, samples are fixed (e.g., with cold 4% paraformaldehyde) and used for phosflow. Surface staining is used to distinguish T and B cells using antibodies directed to cell surface markers that are known to the art. The level of phosphorylation of kinase substrates such as Akt and S6 are then measured by incubating the fixed cells with labeled antibodies specific to the phosphorylated isoforms of these proteins. The population of cells are then analyzed by flow cytometry. Example 231: Colony Formation Assay [00489] Murine bone marrow cells freshly transformed with a pl90 BCR-Abl retrovirus (herein referred to as pi 90 transduced cells) are plated in the presence of various drug combinations in M3630 methylcellulose media for about 7 days with recombinant human IL-7 in about 30% serum, and the number of colonies formed is counted by visual examination under a microscope. [00490] Alternatively, human peripheral blood mononuclear cells are obtained from Philadelphia chromosome positive (Ph+) and negative (Ph-) patients upon initial diagnosis or relapse. Live cells are isolated and enriched for CD19+ CD34+ B cell progenitors. After overnight liquid culture, cells are plated in methocult GF+ H4435 (Stem Cell Technologies), supplemented with cytokines (IL-3, IL-6, IL-7, G-CSF, GM-CSF, CF, Flt3 ligand, and erythropoietin) and various concentrations of known chemotherapeutic agents in combination with compounds of the present disclosure. Colonies are counted by microscopy 12-14 days later. This method can be used to test for evidence of additive or synergistic activity. Example 232: In Vivo Effect of Kinase Inhibitors on Leukemic Cells [00491] Female recipient mice are lethally irradiated from a γ source in two doses about 4 hr apart, with approximately 5Gy each. About 1 hr after the second radiation dose, mice are injected i.v. with about lx 10 6 leukemic cells (e.g., Ph+ human or murine cells, or pl90 transduced bone marrow cells). These cells are administered together with a radioprotective dose of about 5x 10 6 normal bone marrow cells from 3-5 week old donor mice. Recipients are given antibiotics in the water and monitored daily. Mice who become sick after about 14 days are euthanized and lymphoid organs are harvested for analysis. Kinase inhibitor treatment begins about 10 days after leukemic cell injection and continues daily until the mice become sick or a maximum of approximately 35 days post-transplant. Inhibitors are given by oral lavage. [00492] Peripheral blood cells are collected approximately on day 10 (pre -treatment) and upon euthanization (post treatment), contacted with labeled anti-hCD4 antibodies and counted by flow cytometry. This method can be used to demonstrate that the synergistic effect of one or more compounds provided herein in combination with known chemotherapeutic agents can reduce leukemic blood cell counts as compared to treatment with known chemotherapeutic agents (e.g., Gleevec) alone under the conditions tested. Example 233: Treatment of Lupus Disease Model Mice [00493] Mice lacking the inhibitory receptor FcyRIIb that opposes PI3K signaling in B cells develop lupus with high penetrance. FcyRIIb knockout mice (R2KO, Jackson Labs) are considered a valid model of the human disease as some lupus patients show decreased expression or function of FcyRIIb (S. Bolland and J.V. Ravtech 2000. Immunity 12:277-285). [00494] The R2KO mice develop lupus-like disease with anti-nuclear antibodies, glomerulonephritis and proteinurea within about 4-6 months of age. For these experiments, the rapamycin analogue RAD001 (available from LC Laboratories) is used as a benchmark compound, and administered orally. This compound has been shown to ameliorate lupus symptoms in the B6.Slelz.Sle3z model (T. Wu et al. J. Clin Invest. 117:2186-2196). [00495] The NZB/W Fl mice spontaneously develop a systemic autoimmune disease with that is a model of lupus. The mice are treated starting at 20 weeks of age for a profilactic model and at 23 weeks of age for a therapeutic model. Blood and urine samples are obtained throughout the testing period, and tested for antinuclear antibodies (in dilutions of serum) or protein concentration (in urine). Serum is also tested for anti-ssDNA and anti- dsDNA antibodies by ELISA. Glomerulonephritis is assessed in kidney sections stained with H&E at the end of the study, or survival can be an endpoint. For example, the proteozome inhibitor Bortezimib is effective at blocking disease in the NZB/W model in both the profilactic and therapeutic model with reductions in auto-antibody production, kidney damage, and improvements in survival (Nature Medicine 14, 748-755 (2008)). [00496] Lupus disease model mice such as R2KO, BXSB or MLR/lpr are treated at about 2 months old, approximately for about two months. Mice are given doses of: vehicle, RADOOl at about 10 mg/kg, or compounds provided herein at approximately 1 mg/kg to about 500 mg/kg. Blood and urine samples are obtained throughout the testing period, and tested for antinuclear antibodies (in dilutions of serum) or protein concentration (in urine). Serum is also tested for anti-ssDNA and anti-dsDNA antibodies by ELISA. Animals are euthanized at day 60 and tissues harvested for measuring spleen weight and kidney disease. Glomerulonephritis is assessed in kidney sections stained with H&E. Other animals are studied for about two months after cessation of treatment, using the same endpoints. [00497] This established art model can be employed to demonstrate that the kinase inhibitors provided herein can suppress or delay the onset of lupus symptoms in lupus disease model mice. Example 234: Murine Bone Marrow Transplant Assay [00498] Female recipient mice are lethally irradiated from a γ ray source. About 1 hr after the radiation dose, mice are injected with about 1x106 leukemic cells from early passage pl90 transduced cultures (e.g., as described in Cancer Genet Cytogenet. 2005 Aug; 161(1):51 6). These cells are administered together with a radioprotective dose of approximately 5x 10 6 normal bone marrow cells from 3-5 wk old donor mice. Recipients are given antibiotics in the water and monitored daily. Mice who become sick after about 14 days are euthanized and lymphoid organs harvested for flow cytometry and/or magnetic enrichment. Treatment begins on approximately day 10 and continues daily until mice become sick, or after a maximum of about 35 days post- transplant. Drugs are given by oral gavage (p.o.). In a pilot experiment, a dose of chemotherapeutic that is not curative but delays leukemia onset by about one week or less is identified; controls are vehicle-treated or treated with chemotherapeutic agent, previously shown to delay but not cure leukemogenesis in this model (e.g., imatinib at about 70 mg kg twice daily). For the first phase, pl90 cells that express eGFP are used, and postmortem analysis is limited to enumeration of the percentage of leukemic cells in bone marrow, spleen and lymph node (LN) by flow cytometry. In the second phase, pi 90 cells that express a tailless form of human CD4 are used and the postmortem analysis includes magnetic sorting of hCD4+ cells from spleen followed by immunoblot analysis of key signaling endpoints: p Akt -T308 and S473; pS6 and p4EBP-l . As controls for immunoblot detection, sorted cells are incubated in the presence or absence of kinase inhibitors of the present disclosure inhibitors before lysis. Optionally, \"phosflow\" is used to detect p Akt -S473 and pS6-S235/236 in hCD4-gated cells without prior sorting. These signaling studies are particularly useful if, for example, drug-treated mice have not developed clinical leukemia at the 35 day time point. Kaplan-Meier plots of survival are generated and statistical analysis done according to methods known in the art. Results from pi 90 cells are analyzed separated as well as cumulatively. [00499] Samples of peripheral blood (100-200 μΐ ^ ) are obtained weekly from all mice, starting on day 10 immediately prior to commencing treatment. Plasma is used for measuring drug concentrations, and cells are analyzed for leukemia markers (eGFP or hCD4) and signaling biomarkers as described herein. [00500] This general assay known in the art can be used to demonstrate that effective therapeutic doses of the compounds provided herein can be used for inhibiting the proliferation of leukemic cells. Example 235: Matrigel Plug Angiogenesis Assay [00501] Matrigel containing test compounds are injected subcutaneously or intraocularly, where it solidifies to form a plug. The plug is recovered after 7-21 days in the animal and examined histologically to determine the extent to which blood vessels have entered it. Angiogenesis is measured by quantification of the vessels in histologic sections. Alternatively, fluorescence measurement of plasma volume is performed using fluorescein isothiocyanate (FITC)-labeled dextran 150. The results are expected to indicate one or more compounds provided herein that inhibit angiogenesis and are thus expected to be useful in treating ocular disorders related to aberrant angiogenesis and/or vascular permeability. Example 236: Corneal Angiogenesis Assay [00502] A pocket is made in the cornea, and a plug containing an angiogenesis inducing formulation (e.g., VEGF, FGF, or tumor cells), when introduced into this pocket, elicits the ingrowth of new vessels from the peripheral limbal vasculature. Slow-release materials such as EL VAX (ethylene vinyl copolymer) or Hydron are used to introduce angiogenesis inducing substances into the corneal pocket. Alternatively, a sponge material is used. [00503] The effect of putative inhibitors on the locally induced (e.g., sponge implant) angiogenic reaction in the cornea (e.g., by FGF, VEGF, or tumor cells). The test compound is administered orally, systemically, or directly to the eye. Systemic administration is by bolus injection or, more effectively, by use of a sustained- release method such as implantation of osmotic pumps loaded with the test inhibitor. Administration to the eye is by any of the methods described herein including, but not limited to eye drops, topical administration of a cream, emulsion, or gel, intravitreal injection. [00504] The vascular response is monitored by direct observation throughout the course of the experiment using a stereomicroscope in mice. Definitive visualization of the corneal vasculature is achieved by administration of fluorochrome-labeled high-molecular weight dextran. Quantification is performed by measuring the area of vessel penetration, the progress of vessels toward the angiogenic stimulus over time, or in the case of fluorescence, histogram analysis or pixel counts above a specific (background) threshold. [00505] The results can indicate one or more compounds provided herein inhibit angiogenesis and thus can be useful in treating ocular disorders related to aberrant angiogenesis and/or vascular permeability. Example 237: Microtiter-plate Angiogenesis Assay [00506] The assay plate is prepared by placing a collagen plug in the bottom of each well with 5-10 cell spheroids per collagen plug each spheroid containing 400-500 cells. Each collagen plug is covered with 1100 μΕ of storage medium per well and stored for future use (1-3 days at 37 °C, 5% C0 2 ). The plate is sealed with sealing. Test compounds are dissolved in 200 μΕ assay medium with at least one well including a VEGF positive control and at least one well without VEGF or test compound as a negative control. The assay plate is removed from the incubator and storage medium is carefully pipeted away. Assay medium containing the test compounds are pipeted onto the collagen plug. The plug is placed in a humidified incubator for (37 °C, 5% C0 2 ) 24-48 hours. Angiogenesis is quantified by counting the number of sprouts, measuring average sprout length, or determining cumulative sprout length. The assay can be preserved for later analysis by removing the assay medium, adding 1 mL of 10% paraformaldehyde in Hanks BSS per well, and storing at 4 °C. The results are expected to identify compounds that inhibit angiogenesis in various cell types tested, including cells of ocular origin. Example 238: Combination Use of PI3K-6 Inhibitors and Agents that Inhibit IgE Production or Activity [00507] The compounds as provided herein can present synergistic or additive efficacy when administered in combination with agents that inhibit IgE production or activity. Agents that inhibit IgE production include, for example, one or more of TEI-9874, 2-(4-(6-cyclohexyloxy-2-naphtyloxy)phenylacetamide)benzoic acid, rapamycin, rapamycin analogs (i.e., rapalogs), TORC1 inhibitors, TORC2 inhibitors, and any other compounds that inhibit mTORCl and mTORC2. Agents that inhibit IgE activity include, for example, anti-IgE antibodies such as Omalizumab and TNX-901. [00508] One or more of the subject compounds capable of inhibiting PI3K-6 can be efficacious in treatment of autoimmune and inflammatory disorders (AIID), for example, rheumatoid arthritis. If any of the compounds causes an undesired level of IgE production, one can choose to administer it in combination with an agent that inhibits IgE production or IgE activity. Additionally, the administration of PI3K-6 or ΡΙ3Κ-δ/γ inhibitors as provided herein in combination with inhibitors of mTOR can also exhibit synergy through enhanced inhibition of the PI3K pathway. Various in vivo and in vitro models can be used to establish the effect of such combination treatment on AIID including, but not limited to: (a) in vitro B-cell antibody production assay, (b) in vivo TNP assay, and (c) rodent collagen induced arthritis model. (a) B-cell Assay [00509] Mice are euthanized, and the spleens are removed and dispersed through a nylon mesh to generate a single-cell suspension. The splenocytes are washed (following removal of erythrocytes by osmotic shock) and incubated with anti-CD43 and anti-Mac- 1 antibody-conjugated microbeads (Miltenyi Biotec). The bead-bound cells are separated from unbound cells using a magnetic cell sorter. The magnetized column retains the unwanted cells and the resting B cells are collected in the flow-through. Purified B-cells are stimulated with lipopolysaccharide or an anti-CD40 antibody and interleukin 4. Stimulated B-cells are treated with vehicle alone or with PI3K-6 inhibitors as provided herein with and without mTOR inhibitors such as rapamycin, rapalogs, or mTORCl/C2 inhibitors. The results are expected to show that in the presence of mTOR inhibitors (e.g., rapamycin) alone, there is little to no substantial effect on IgG and IgE response. However, in the presence of PI3K-6 and mTOR inhibitors, the B-cells are expected to exhibit a decreased IgG response as compared to the B-cells treated with vehicle alone, and the B- cells are expected to exhibit a decreased IgE response as compared to the response from B-cells treated with PI3K-6 inhibitors alone. (b) TNP Assay [00510] Mice are immunized with TNP-Ficoll or TNP-KHL and treated with: vehicle, a PI3K-6 inhibitor, an mTOR inhibitor, for example rapamycin, or a PI3K-6 inhibitor in combination with an mTOR inhibitor such as rapamycin. Antigen-specific serum IgE is measured by ELISA using TNP-BSA coated plates and isotype specific labeled antibodies. It is expected that mice treated with an mTOR inhibitor alone exhibit little or no substantial effect on antigen specific IgG3 response and no statistically significant elevation in IgE response as compared to the vehicle control. It is also expected that mice treated with both PI3K-6 inhibitor and mTOR inhibitor exhibit a reduction in antigen specific IgG3 response as compared to the mice treated with vehicle alone. Additionally, the mice treated with both PI3K-6 inhibitor and mTOR inhibitor exhibit a decrease in IgE response as compared to the mice treated with PI3K-6 inhibitor alone. (c) Rat Collagen Induced Arthritis Model [00511] Female Lewis rats are anesthetized and given collagen injections prepared and administered as described previously on day 0. On day 6, animals are anesthetized and given a second collagen injection. Caliper measurements of normal (pre-disease) right and left ankle joints are performed on day 9. On days 10-11, arthritis typically occurs and rats are randomized into treatment groups. Randomization is performed after ankle joint swelling is obviously established and there is good evidence of bilateral disease. [00512] After an animal is selected for enrollment in the study, treatment is initiated. Animals are given vehicle, PI3K-6 inhibitor, or PI3K-6 inhibitor in combination with rapamycin. Dosing is administered on days 1-6. Rats are weighed on days 1-7 following establishment of arthritis and caliper measurements of ankles taken every day. Final body weights are taken on day 7 and animals are euthanized. [00513] The combination treatment using a compound as provided herein and rapamycin can provide greater efficacy than treatment with PI3K-6 inhibitor alone. Example 239: Delayed Type Hypersensitivity Model [00514] DTH is induced by sensitizing 60 BALB/c male mice on day 0 and day 1 with a solution of 0.05% 2,4 dinitrofluorobenzene (DNFB) in a 4: 1 acetone/olive oil mixture. Mice are gently restrained while 20 μΕ of solution is applied to the hind foot pads of each mouse. The hind foot pads of the mice are used as they represent an anatomical site that can be easily isolated and immobilized without anesthesia. On day 5, mice are administered a single dose of vehicle, a compound provided herein at 10, 3, 1, or 0.3 mg/kg, or dexamethasone at a dose of 5 mg/kg by oral gavage. Thirty minutes later mice are anaesthetized, and a solution of 0.25% DNFB in a 4: 1 acetone/olive oil solution is applied to the left inner and outer ear surface. This application results in the induction of swelling to the left ear and under these conditions, all animals responded to this treatment with ear swelling. A vehicle control solution of 4: 1 acetone/olive oil is applied to the right inner and outer ear. Twenty four hours later, mice are anaesthetized, and measurements of the left and right ear are taken using a digital micrometer. The difference between the two ears is recorded as the amount of swelling induced by the challenge of DNFB. Drug treatment groups are compared to vehicle control to generate the percent reduction in ear swelling. Dexamethasone is routinely used as a positive control as it has broad anti-inflammatory activity. Example 240: Peptidoglycan-Polysaccharide rat Arthritic Model (a) Systemic arthritis model [00515] All injections are performed under anesthesia. 60 female Lewis rats (150-170) are anesthetized by inhalation isoflurane using a small animal anesthesia machine. The animals are placed in the induction chamber until anesthetized by delivery of 4-5% isoflurane in (¾ and then held in that state using a nose cone on the procedure table. Maintenance level of isoflurane is at 1-2%. Animals are injected intraperitoneally (i.p.) with a single injection of purified PG-PS 10S Group A, D58 strain (concentration 25 μg/g of bodyweight) suspended in sterile 0.85% saline. Each animal receives a total volume of 500 microliters administered in the lower left quadrant of the abdomen using a 1 milliliter syringe with a 23 gauge needle. Placement of the needle is critical to avoid injecting the PG-PS 10S into either the stomach or caecum. Animals are under continuous observation until fully recovered from anesthesia and moving about the cage. An acute response of a sharp increase in ankle measurement, typically 20% above baseline measurement can peak in 3-5 days post injection. Treatment with test compounds can be PO, SC, r or IP. Rats are dosed no more than two times in a 24 hour time span. Treatment can begin on day 0 or any day after that through day 30. The animals are weighed on days 0, 1, 2, 3, 4, 5, 6, 7 and beginning again on day 12-30 or until the study is terminated. Paw/ankle diameter is measured with a digital caliper on the left and right side on day 0 prior to injection and again on day 1, 2, 3, 4, 5, 6 and 7. On day 12, measurements begin again and continue on through day 30. At this time, animals can be anesthetized with isoflurane, as described above, and terminal blood samples can be obtained by tail vein draws for the evaluation of the compound blood levels, clinical chemistry or hematology parameters. Animals are then euthanized with carbon dioxide overdose. A thoracotomy can be conducted as a means of death verification. (b) Monoarticular arthritis model [00516] All injections are performed under anesthesia. 60 female Lewis rats (150-170) are anesthetized by inhalation isoflurane using a small animal anesthesia machine. The animals are placed in the induction chamber until anesthetized by delivery of 4-5 % isoflurane in (¾ and then held in that state using a nose cone on the procedure table. Maintenance level of isoflurane is at 1-2%. Animals are injected intra- articular (i.a.) with a single injection of purified PG-PS 100P Group A, D58 strain (concentration 500 μg/mL) suspended in sterile 0.85% saline. Each rat receives a total volume of 10 microliters administered into the tibiotalar joint space using a 1 milliliter syringe with a 27 gauge needle. Animals are under continuous observation until fully recovered from anesthesia and moving about the cage. Animals that respond 2-3 days later with a sharp increase in ankle measurement, typically 20% above baseline measurement on the initial i.a. injection, are included in the study. On day 14, all responders are anesthetized again using the procedure previously described. Animals receive an intravenous (I.V.) injection of PG-PS (concentration 250 μΕ/ηιί). Each rat receives a total volume of 400 microliters administered slowly into the lateral tail vein using a 1 milliliter syringe with a 27 gauge needle. Baseline ankle measurements are measured prior to IV injection and continue through the course of inflammation or out to day 10. Treatment with test compounds will be PO, SC, IV or IP. Rats are dosed no more than two times in a 24 hour time span. Treatment can begin on day 0 or any day after that through day 24. The animals are weighed on days 0, 1, 2, 3, 4, 5, and beginning again on day 14-24 or until the study is terminated. Paw/ankle diameter is measured with a digital caliper on the left and right side on day 0 prior to injection and again on day 1, 2, 3, 4, 5, and beginning again on day 14-24 or until the study is terminated. At this time, animals can be anesthetized with isoflurane, as described above, and terminal blood samples can be obtained by tail vein draws for the evaluation of the compound blood levels, clinical chemistry or hematology parameters. Animals are them euthanized with carbon dioxide overdose. A thoracotomy can be conducted as a means of death verification. Example 241: Mice Models for Asthma [00517] Efficacy of a compound provided herein in treating, preventing and/or managing asthma can be assessed using an conventional animal models including various mice models described in, for example, Nials et al., Dis Model Mech. 1(4-5): 213-220 (2008). (a) Acute Allergen Challenge Models [00518] Several models are known in the art and any of such models can be used. Although various allergens can be used to induce asthma-like conditions, the principle is consistent throughout the methods. Briefly, asthma- like conditions are induced through multiple systemic administration of the allergen (e.g. , ova, house dust mite extracts and cockroach extracts) in the presence of an adjuvant such as aluminum hydroxide. Alternatively, an adjuvant-free system can be used, but it usually requires a higher number of exposures to achieve suitable sensitization. Once induced, animals exhibit many key features of clinical asthma such as: elevated levels of IgE; airway inflammation; goblet cell hyperplasia; epithelial hypertrophy; AHR ro specific stimuli; and early and late phase bronchoconstriction. Potential efficacy of a compound thus can be assessed by determining whether one or more of these clinical features are reversed or mitigated. (b) Chronic Allergen Challenge Models [00519] Chronic allergen challenge models aim to reproduce more of the features of the clinical asthma, such as airway remodeling and persistent AHR, than acute challenge models. While allergens similar to those used in acute allergen challenge models can be used, in chronic allergen challenge models, animals are subjected to repeated exposure of the airways to low levels of allergen for a period of up to 12 weeks. Once induced, animals exhibit key features of human asthma such as: allergen-dependent sensitization; a Th2-dependent allergic inflammation characterized by eosinophillic influx into the airway mucosa; AHR; and airway remodeling as evidenced by goblet cell hyperplasia, epithelial hypertrophy, subepithelial or peribronchiolar fibrosis. Potential efficacy of a compound thus can be assessed by determining whether one or more of these clinical features are reversed or mitigated. Example 242: Models for Psoriasis [00520] Efficacy of a compound provided herein in treating, preventing and/or managing psoriasis can be assessed using an conventional animal models including various animal models described in, for example, Boehncke et al., Clinics in Dermatology, 25: 596-605 (2007). [00521 ] As an example, the mouse model based on adoptive transfer of CD4 + CD45RB hl T cells described in Hong et al, J. Immunol, 162: 7480-7491 (1999) can be made. Briefly, female BALB/cBY (donor) and C.B.- 17/Prkdc scid/scid (recipient) mice are housed in a specific pathogen-free environment and are used between 6 and 8 weeks of age. CD4 + T cells are enriched from BALB/cBy splenocytes using a mouse CD4 enrichment kit. The cells are then labeled with PE-conjugated anti-CD4, FITC-conjugated anti-CD45RB, and APC-conjugated anti- CD25 antibodies. Cells are sorted using a cell sorter. CD4 + CD45RB hi CD25 cells are collected. Cells are resuspended in saline and 4x 10 8 cells/mouse are injected i.p. into C.B.-17/Prkdc scid/scid mice. Mice can be dosed with LPS, cytokines, or antibodies as necessary. Mice are monitored for external signs of skin lesions twice each week. After the termination, ear, back skin, lymph nodes and spleen can be collected for further ex vivo studies. Example 243: Models for Scleroderma [00522] A compound's efficacy in treating scleroderma can be tested using animal models. An exemplary animal model is a mouse model for scleroderma induced by repeated local injections of bleomycin (\"BLM\") described, for example, in Yamamoto et ah, J Invest Dermatol 112: 456-462 (1999), the entirety of which is incorporated herein by reference. This mouse model provides dermal sclerosis that closely resembles systemic sclerosis both histologically and biochemically. The sclerotic changes observed in the model include, but are not limited to: thickened and homogenous collagen bundles and cellular filtrates; gradual increase in number of mast cells; degranulation of mast cells; elevated histamine release; increase in hydroxyproline in skin; presence of anti- nuclear antibody in serum; and strong expression of transforming growth factor β-2 mRNA. Therefore, efficacy of a compound in treating scleroderma can be assessed by monitoring the lessening of one or more of these changes. [00523] Briefly, the following exemplary procedures can be used to generate the mouse model for scleroderma: Specific pathogen-free, female BALB/C mice and C3H mice of 6 weeks old, weighing about 20 g, are purchased and maintained with food and water ad libitum. BLM is dissolved in PBS at differing concentrations and sterilized with filtration. Aliquots of each concentration of BLM or PBS are injected subcutaneously into the shaved back of the mice daily for 1-4 weeks with a needle. Alternatively, mice are injected every other day. [00524] Histolopathological and biochemical changes induced can be assessed using any methods commonly practiced in the field. For example, histopathological changes can be assessed using a standard avidine- biotin peroxidase technique with anti-L3T4 monoclonal antibody, anti-Lyt2 monoclonal antibody, anti-mouse pan- tissue-fixed macrophage antibody, anti-stem cell factor monoclonal antibody, anti-transforming growth factor-β polyclonal antibody, and anti-decorin antibody. Cytokine expression of cellular infiltrates can be assessed by using several anti-cytokine antibodies. Hydroxyproline level can be assessed by hydrolyzing skin pieces with hydrochloric acid, neutralizing with sodium hydroxide, and colorimetrically assessing the hydrolates at 560 nm with p-dimethylaminobenzaldehyde. Pepsin-resistant collagen can be assessed by treating collagen sample extracted from biopsied tissues and analyzing by polyacrylamide stacking gel electrophoresis. Mast cells can be identified by toluidine blue, and cells containing matachromatic granules can be counted under high magnification of a light microscope. Serum levels of various cytokines can be assessed by enzyme-linked immunosorbent assay, and mRNA levels of the cytokines can be assessed by reverse-transcriptase polymerase chain reaction. Autoantibodies in serum can be detected using 3T3 fibroblasts as the substrate for the screening. Example 244: Models for Myositis [00525] A compound's efficacy in treating myositis (e.g. , dermatomyositis) can be tested using animal models known in the art. One such example is the familial canine dermatomyositis model described in Hargis et ah, AJP 120(2): 323-325 (1985). Another example is the rabbit myosin induced mouse model described in Phyanagi et al, Arthritis & Rheumatism, 60(10): 3118-3127 (2009). [00526] Briefly, 5-week old male SJL/J mice are used. Purified myosin from rabbit skeletal muscle (6.6 mg/ml) is emulsified with an equal amount of Freund's complete adjuvant and 3.3 mg/ml Mycobacterium butyricum. The mice are immunized repeatedly with emulsified rabbit myosin. Once myositis is induced, inflammatory cell filtration and necrotic muscle fiber should be evident in the model. In the muscles of animals, CD4 + T cells are mainly located in the perimysum and CD8 + T cells are mainly located in the endomysium and surround non-necrotic muscle fibers. TNFa, IFNy and perforin are up-regulated and intercellular adhesion molecule 1 is increased in the muscles. [00527] To assess the efficacy of a compound, following administration of the compound through adequate route at specified dose, the mice are killed and muscle tissues are harvested. The muscle tissue is immediately frozen in chilled isopentane precooled in liquid nitrogen, and then cryostat sections are prepared. The sections are stained with hematoxylin and eosin for counting of number of infiltrated cells. Three sections from each mouse are prepared and photomicrographs are obtained. For immunohistochemical tests, cryostat sections of muscle are dried and fixed in cold acetone at -20 °C. The slides are rehydrated in PBS, and then endogeneous peroxide activity is blocked by incubation in 1% hydrogen peroxide. The sections are incubated overnight with rat anti-mouse CD4 monoclonal antibody, rat anti-mouse CD8 monoclonal antibody, rat anti-mouse F4/80 monoclonal antibody or normal rat IgG in antibody diluent. The samples are washed with PBS and incubated with biotin- conjugated rabbit anti-rat IgG pretreated with 5% normal mouse serum. After washing with PBS, the samples are incubated with streptavidin-horseradish peroxidase. After washing PBS, diaminobenzidine is used for visualization. Example 245: Models for Sjogren Syndrome [00528] A compound's efficacy in treating Sjogren's syndrome can be tested using animal models known in the art, for example, those described in Chiorini et al., Journal of Autoimmunity 33: 190-196 (2009). Examples include: mouse model spontaneously developed in first filial generation of NZB mice crossed to NZW mice {see, e.g., Jonsson et al., Clin Immunol Immunopathol 42: 93-101 (1987); mouse model induced by i.p. injection of incomplete Freund's adjuvant {id.; Deshmukh et al., J Oral Pathol Med 38: 42-27 (2009)); NOD mouse models wherein Sjogren's phenotype is developed by specific genotypes {see, e.g., Cha et ah, Arthritis Rheum 46: 1390- 1398 (2002); Kong et al, Clin Exp Rheumatol 16: 675-681 (1998); Podolin et al, J Exp Med 178: 793-803 (1993); and Rasooly et al., Clin Immunol Immunopathol 81 : 287-292 (1996)); mouse model developed in spontaneous lpr mutation; mouse model developed in Id3 knock-out mice {see, e.g. , Li et al., Immunity 21 : 551-560 (2004)); mouse model developed in PI3K knock-out mice {see, e.g. , Oak et al., Proc Natl Acad Sci USA 103 : 16882- 16887 (2006)); mouse model developed in BAFF over-expressing transgenic mice {see, e.g., Groom et al., J Clin Invest 109: 59-68 (2002)); mouse model induced by injection of Ro antigen into BALB/c mice {see, e.g., Oh-Hora et al., Nat. Immunol 9: 432-443 (2008)); mouse model induced by injection of carbonic anhydrase II {see, e.g., Nishimori et al., J Immunol 154: 4865-4873 (1995); mouse model developed in IL-14 over-expressing transgenic mice {see, e.g., Shen et al., J Immunol 177: 5676-5686 (2006)); and mouse model developed in IL-12 expressing transgenic mice {see, e.g. , McGrath-Morrow et al., Am J Physiol Lung Cell Mol Physiol 291 : L837-846 (2006)). Example 246: Models for Immune Complex Mediated Disease [00529] The Arthus reaction is a type 3 immune response to immune complexes, and thus, can be a mechanistic model supporting therapeutic hypothesis for immune complex mediated diseases such as rheumatoid arthritis, lupus and other autoimmune diseases. For example, ΡΙ3Κγ and δ deficient mice can be used as experimental models of the Arthus reaction and provide assessment of therapeutic potential of a compound as to the treatment of immune complex mediated diseases. The Arthus reaction can be induced using the following exemplary procedures as described in Konrad et al., Journal of Biological Chemistry (2008 283(48): 33296-33303. [00530] ΡΙ3Κγ- and PI3K6-deficient mice are maintained under dry barrier conditions. Mice are anesthetized with ketamine and xylazine, and the trachea is cannulated. Appropriate amount of protein G-purified anti-OVA IgG Ab is applied, and appropriate amount of OVA antigen is given intravenously. For PI3K blocking experiments, wortmanin is given intratracheally together with the application of anti-OVA igG. Mice are killed at 2-4 hours after initiation of inflammation, and desired follow up assessments can be performed using methods known in the art. Example 247: PI3-Kinase Promega™ Assay [00531] Promega ADP-Glo Max assay kit (Cat. No. V7002) was utilized to determine IC 50 values for α, β, δ and γ isoforms of human Class I PI3 kinases (Millipore). Samples of kinase (20 nM a or δ, 40 nM β or γ isoform) were incubated with compound for 15 minutes at room temperature in reaction buffer (15 mM HEPES pH 7.4, 20 mM NaCl, 1 mM EGTA, 0.02% Tween 20, 10 mM MgCl 2 , 0.2 mg/mL bovine-y-globulins) followed by addition of ATP/diC8-PtdInsP mixture to give final concentrations of 3 mM ATP and 500 uM diC 8 -PtdInsP. Reactions were incubated at room temperature for 2 hours followed by addition of 25 uL of stop solution. After a 40-minute incubation at room temperature, 50 uL of Promega detection mix was added followed by incubation for 1 hour at room temperature. Plates were then read on Envision plate reader in luminescence mode. Data was converted to % inhibition using the following equation below: %inhibition = 100 - where S is the sample luminescence, Pos is a positive control without added PI3K, Neg is the negative control without added compound. Data was then plotted as % inhibition vs compound concentration. Data fit to 4 parameter logistic equation to determine IC 50 values: max— min % Inhibition [I]h [00532] Certain compounds provided herein were tested in PI3-Kinase Promega Assay using procedures as described above to determine IC 50 values for α, β, δ and/or γ isoforms. The IC 50 values are summarized in Table 7. Example 248: Isoform-Selective Cellular Assays (a) PI3K-S Selective Assay [00533] A compound's ability in selectively inhibiting PI3K-6 can be assessed using RAJI cells, i.e. , B lymphocyte cells derived from lymphoma patients. Briefly, serum-starved RAJI cells are stimulated with anti- human IgM, thereby causing signaling through the B-cell receptors, as described in, for example, He et al., Leukemia Research (2009) 33: 798-802. B-cell receptor signaling is important for the activation, differentiation, and survival of B cells and certain B-cell derived cancers. Reduction of phospho-AKT is indicative of compounds that can inhibit B-cell proliferation and function in certain diseases. By monitoring the reduction of phospho-AKT in stimulated RAJI cells (using for example, phospho-AKT antibodies), a compound's potential efficacy in selectively inhibiting PI3K6 can be assessed. [00534] Certain compounds provided herein were tested in RAJI cell model using procedures as described above. The IC 50 values for phospho-AKT are summarized in Table 7. (b) PI3K-y Selective Assay [00535] A compound's ability in selectively inhibiting ΡΙ3Κ-γ can be assessed using RAW264.7 macrophages. Briefly, serum-starved RAW264.7 cells are stimulated with a known GPCR agonist C5a. See, e.g., Camps et al., Nature Medicine (2005) l l(9):936-943. Cells can be treated with test compounds prior to, simultaneously with, or subsequent to the stimulation by C5a. RAW 264.7 cells respond to the complement component fragment C5a through activation of the C5a receptor, and the C5a receptor activates macrophages and induces cell migration. Test compounds' ability to inhibit C5a-mediated AKT phosphorylation is indicative of selective inhibition of ΡΙ3Κ-γ. Thus, by monitoring the reduction of phospho-AKT in stimulated RAW 264.7 cells (using for example, phospho-AKT antibodies), a compound's potential efficacy in selectively inhibiting ΡΒΚγ can be assessed. [00536] Certain compounds provided herein were tested in RAW 264.7 cell model using procedures as described above. The IC 50 values for phospho-AKT are summarized in Table 7. (c) PI3K-a Selective Assay [00537] A compound's ability in selectively inhibiting PI3K-a can be assessed using SKOV-3 cells, i.e., human ovarian carcinoma cell line. Briefly, SKOV-3 cells, in which mutant PDKa is constitutively active, can be treated with test compounds. Test compounds' ability to inhibit AKT phosphorylation in SKOV-3 cells, therefore, is indicative of selective inhibition of PI3Ka. Thus, by monitoring the reduction of phospho-AKT in SKOV-3 cells (using for example, phospho-AKT antibodies), a compound's potential efficacy in selectively inhibiting ΡΙ3Κα can be assessed. (d) ΡΙ3Κ-β Selective Assay [00538] A compound's ability in selectively inhibiting ΡΙ3Κ-β can be assessed using 786-0 cells, i.e. , human kidney carcinoma cell line. Briefly, 786-0 cells, in which ΡΙ3Κβ is constitutively active, can be treated with test compounds. Test compounds' ability to inhibit AKT phosphorylation in 786-0 cells, therefore, is indicative of selective inhibition of ΡΙ3Κβ. 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enantiomeric excess of greater than about 25%, greater than about 30%, greater than about 40%, greater than about 50%, greater than about 60%, greater than about \n\n 70%, greater than about 80%, greater than about 85%, greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%."],"number":4,"annotation":false,"title":false,"claim":true},{"lines":["The compound of claim 4, wherein the enantiomeric excess is greater than about 90%, greater than about 95%, greater than about 97%, greater than about 98%, or greater than about 99%."],"number":5,"annotation":false,"title":false,"claim":true},{"lines":["The compound of claim 5, wherein the enantiomeric excess is greater than about 97%, greater than about 98%, or greater than about 99%."],"number":6,"annotation":false,"title":false,"claim":true},{"lines":["The compound of any of claims 1 -6, wherein the pharmaceutically acceptable form is a salt or a solvate."],"number":7,"annotation":false,"title":false,"claim":true},{"lines":["The compound of any of claims 1-7, wherein the pharmaceutically acceptable form is a salt."],"number":8,"annotation":false,"title":false,"claim":true},{"lines":["The compound of any of claims 1-7, wherein the pharmaceutically acceptable form is a solvate."],"number":9,"annotation":false,"title":false,"claim":true},{"lines":["A compound, wherein the compound is selected from a compound in Table 1, Table 2, Table 2, Table 3, Table 4, Table 5, or Table 6."],"number":10,"annotation":false,"title":false,"claim":true},{"lines":["A pharmaceutical composition comprising a compound of any of claims 1-10, and a pharmaceutically acceptable excipient, diluent, or carrier."],"number":11,"annotation":false,"title":false,"claim":true},{"lines":["A method of treating or preventing a PI3K mediated disorder in a subject, the method comprising administering a therapeutically effective amount of a compound of any of claims 1-10 or a composition of claim 11 to said subject."],"number":12,"annotation":false,"title":false,"claim":true},{"lines":["Use of a compound of any of claims 1 - 10 in the manufacture of a medicament for treating or preventing a PI3K mediated disorder in a subject."],"number":13,"annotation":false,"title":false,"claim":true},{"lines":["A compound of any of claims 1-10 for use in treating or preventing a PI3K mediated disorder in a subject."],"number":14,"annotation":false,"title":false,"claim":true},{"lines":["The method, use, or compound of any of claims 12-14, wherein the disorder is cancer, an inflammatory disease, or an auto-immune disease."],"number":15,"annotation":false,"title":false,"claim":true},{"lines":["A method for inhibiting PI3K in a cell or subject comprising contacting the cell or administering to the subject a compound of any of claims 1-10."],"number":16,"annotation":false,"title":false,"claim":true},{"lines":["A process of preparing a (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising:"],"number":17,"annotation":false,"title":false,"claim":true},{"lines":["deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one."],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["The process of claim 17, further comprising:"],"number":18,"annotation":false,"title":false,"claim":true},{"lines":["contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- 1 (2H)-one with 6-chloro-9-(tetrahydro-2H- pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( IS)- 1 -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one."],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["The process of claim 18, further comprising:"],"number":19,"annotation":false,"title":false,"claim":true},{"lines":["contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one."],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["The process of claim 19, further comprising:"],"number":20,"annotation":false,"title":false,"claim":true},{"lines":["contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate."],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["A process of preparing a (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one (Compound Is) comprising: \n\n contacting 2-fluoro-6-methyl-N-phenylbenzamide with (S)-tert-butyl (l-(methoxy(methyl)amino)-l- oxobutan-2-yl)carbamate to form (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3- yl)carbamate;"],"number":21,"annotation":false,"title":false,"claim":true},{"lines":["contacting (S)-tert-butyl (l-(3-fluoro-2-(phenylcarbamoyl)phenyl)-2-oxopentan-3-yl)carbamate with an acid to form (S)-3-(l-aminopropyl)-8-fluoro-2-phenylisoquinolin-l(2H)-one;"],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- 1 (2H)-one with 6-chloro-9-(tetrahydro-2H- pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3 -(( IS)- 1 -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one; and"],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["deprotecting 8-fluoro-2-phenyl-3 -(( 1 S)-l -((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin-l(2H)-one to form (S)-3-(l-((9H-purin-6-yl)amino)propyl)-8-fluoro-2- phenylisoquinolin- 1 (2H)-one."],"number":-1,"annotation":true,"title":false,"claim":false},{"lines":["A process of preparing 8-fluoro-2-phenyl-3-((lS)-l-((9-(tetrahydro-2H-pyran-2-yl)-9H-purin-6- yl)amino)propyl)isoquinolin- 1 (2H)-one comprising contacting (S)-3 -( 1 -aminopropyl)-8-fluoro-2-phenylisoquinolin- l(2H)-one with 6-chloro-9-(tetrahydro-2H-pyran-2-yl)-9H-purine to form 8-fluoro-2-phenyl-3-((lS)-l-((9- (tetrahydro-2H-pyran-2-yl)-9H-purin-6-yl)amino)propyl)isoquinolin-l(2H)-one."],"number":22,"annotation":false,"title":false,"claim":true}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}