USP7-IN-20 

USP7-IN-20 is a highly selective USP7 inhibitor that binds allosterically to the allosteric pocket of USP7 in a non-competitive and reversible manner. USP7-IN-20 downregulates MDM2 protein levels and stabilizes p53, thereby inducing p21 expression and enhancing the ubiquitin-dependent degradation of MDM2. USP7-IN-20 effectively binds endogenous USP7 to inhibit cancer cell proliferation, and also induces apoptosis by promoting the cleavage of PARP and caspase 3. USP7-IN-20 can be widely used in cancer-related basic and translational research.^[1]

USP7-IN-20 (Compound 2) (0.3 μM; 30 min pre-incubation, 90 min assay) potently inhibits full-length USP7 enzyme activity in vitro with an IC₅₀ of 0.3 μM and binds reversibly to the USP7 catalytic domain with a K_d of 2.6 μM^[1].
USP7-IN-20 (0.85 μM; 2 h) potently engages endogenous USP7 in HCT116 colorectal cancer cells with an EC₅₀ of 0.85 μM^[1].
USP7-IN-20 (2.6 μM; 24 h) induces MDM2 ubiquitination in SJSA-1 osteosarcoma cells with an EC₅₀ of 2.6 μM^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

490.41

C₂₂H₂₄BrN₃O₃S

2196246-28-1

O=C1C2=C(C(Br)=CS2)N=CN1CC3(CCN(CC3)C(C[C@H](C4=CC=CC=C4)C)=O)O

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Gavory G, et al. Discovery and characterization of highly potent and selective allosteric USP7 inhibitors. Nat Chem Biol. 2018;14(2):118-125.  [Content Brief]