An inhibitor of PIP3/protein binding
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PIT-1

Item No. 10728

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N-[[(3-chloro-2-hydroxy-5-nitrophenyl)amino]thioxomethyl]-benzamide
CAS Number
53501-41-0
Molecular Formula
C14H10ClN3O4S
Formula Weight
351.8
Purity
≥98%
Formulation (Request formulation change)
A crystalline solid
Solubility(Learn about Variance in Solubility)
DMF: 20 mg/mlDMSO: 20 mg/mlDMSO:PBS (pH 7.2) (1:1): 0.5 mg/mlEthanol: 0.5 mg/ml
λmax
273, 317 nm
SMILES
O=C(NC(NC1=C(O)C(Cl)=CC([N+]([O-])=O)=C1)=S)C2=CC=CC=C2
InChi Code
InChI=1S/C14H10ClN3O4S/c15-10-6-9(18(21)22)7-11(12(10)19)16-14(23)17-13(20)8-4-2-1-3-5-8/h1-7,19H,(H2,16,17,20,23)
InChi Key
RIGXBXPAOGDDIG-UHFFFAOYSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    5 mg

    $22

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    10 mg

    $41

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    50 mg

    $161

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    100 mg

    $283

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    Cayman Chemical
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    Product Description

    PtdIns-(3,4,5)-P3 (PIP3) serves as an anchor for the binding of signal transduction proteins bearing pleckstrin homology (PH) domains such as phosphatidylinositol 3-kinase (PI3K) or PTEN. Protein binding to PIP3 is important for cytoskeletal rearrangement and membrane trafficking and initiates an intricate signaling cascade that has been implicated in cancer.1 PIT-1 is a selective nonphosphoinositide inhibitor that specifically disrupts PIP3/Akt PH domain binding with an IC50 value of 31 μM.2 PIT-1 suppresses PI3K-PDK1-Akt-dependent phosphorylation, which has been shown to reduce cell viability and induce apoptosis in PTEN-deficient U87MG glioblastoma cells (IC50 = 37 μM).2

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Vivanco, I., and Sawyers, C.L. The phosphatidylinositol 3-kinase-AKT pathway in human cancer. Nat. Rev. Cancer 2(7), 489-501 (2002).

    2. Miao, B., Skidan, I., Yang, J., et al. Small molecule inhibition of phosphatidylinositol-3,4,5-triphosphate (PIP3) binding to pleckstrin homology domains. Proc. Natl. Acad. Sci. USA 107(46), 20126-20131 (2010).