An irreversible inhibitor of Cdc25 isoforms
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NSC 95397

Item No. 21431

Technical Information
Formal Name
2,3-bis[(2-hydroxyethyl)thio]-1,4-naphthalenedione
CAS Number
93718-83-3
Synonyms
  • Cdc25 Inhibitor IV
  • PTP Inhibitor XXIX
Molecular Formula
C14H14O4S2
Formula Weight
Purity
≥98%
Formulation
A crystalline solid
DMF: 30 mg/mlDMSO: 30 mg/mlDMSO:PBS (pH 7.2)(1:5): 0.16 mg/mlEthanol: 0.33 mg/ml
λmax
240, 274, 452 nm
SMILES
O=C1C(SCCO)=C(SCCO)C(C2=CC=CC=C21)=O
InChi Code
InChI=1S/C14H14O4S2/c15-5-7-19-13-11(17)9-3-1-2-4-10(9)12(18)14(13)20-8-6-16/h1-4,15-16H,5-8H2
InChi Key
MAASHDQFQDDECQ-UHFFFAOYSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    Product Description

    NSC 95397 is a 1,4-naphthoquinone-based irreversible inhibitor of Cdc25 dual-specificity phosphatases, with Ki values of 32, 96, and 40 nM for Cdc25A, Cdc25B, and Cdc25C, respectively.1 It displays >125-fold selectivity for Cdc25 over VH1-related dual-specificity phosphatase and protein tyrosine phosphatase 1b. NSC 95397 significantly inhibits the growth of human and murine carcinoma cells, blocking G2/M phase transition.1,2 In rat liver epithelial cells, NSC 95397 induces cell cycle arrest, which is associated with phosphorylation of EGFR, activation of ERK1/2, phosphorylation of connexin43, and downregulation of gap junctional intercellular communication.3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Lazo, J.S., Nemoto, K., Pestell, K.E., et alIdentification of a potent and selective pharmacophore for Cdc25 dual specificity phosphatase inhibitors. Mol. Pharmacol. 61(4), 720-728 (2002).

    2. Han, Y., Shen, H., Carr, B.I., et alNAD(P)H:quinone oxidoreductase-1-dependent and -independent cytotoxicity of potent quinone Cdc25 phosphatase inhibitors. J. Pharmacol. Exp. Ther. 309(1), 64-70 (2004).

    3. Melchheier, I., von Montfort, C., Stuhlmann, D., et alQuinone-induced Cdc25A inhibition causes ERK-dependent connexin phosphorylation. Biochem. Biophys. Res. Commun. 327(4), 1016-1023 (2005).