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首页-小分子抑制剂&激动剂-Metabolic Enzyme/Protease-Protein Phosphatase/PTP-DDO-3733
DDO-3733

Chemical Structure : DDO-3733

CAS No.: 2923531-63-7

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DDO-3733 (DDO 3733)

货号: PC-22917Not For Human Use, Lab Use Only.

DDO-3733 is a specific, small molecule, allosteric activator of serine/threonine protein phosphatase 5 (PP5) with potency of 2.9-fold PP5 activation at 50 uM, inhibits HSP90 inhibitor-induced heat shock protein expression both in cells and in vivo.

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纯度 & COA & 质检文件 纯度: >98% (HPLC)

生物&药学活性

DDO-3733 is a specific, small molecule, allosteric activator of serine/threonine protein phosphatase 5 (PP5) with potency of 2.9-fold PP5 activation at 50 uM, inhibits HSP90 inhibitor-induced heat shock protein expression both in cells and in vivo.
DDO-3733 not affect the binding of the TPR-dependent PP5 activator to immobilized PP5 with a verified TPR-independent mechanism.
DDO-3733 shows ITC Kd of 1.14 uM for full-length PP5 binding, and ITC Kd of 0.811 uM of the phosphatase domain, but not to the TPR domain.
DDO-3733 activates PP5 with an EC50 value of 52.8 μM and an Emax value of 4.3-fold.
DDO-3733 does not affect the enzymatic activity of a small panel of phosphatases has been measured, including protein phosphatase 1 α and β (PP1A, PP1B), protein phosphatase 2A (PP2A), protein tyrosine phosphatase nonreceptor type 2 (PTPN2), low molecular weight protein tyrosine phosphatase A (LMPTP-A), dual-specificity phosphatase 3 (DUSP3), and SH2-containing protein tyrosine phosphatase-2 (SHP2).
DDO-3733 induces PP5 substrate dephosphorylation in vitro.
DDO-3733 enhances the antitumor activity of AT13387 and inhibits AT13387 induced expression of heat shock proteins.
AT13387 (20 mg/kg) and DDO-3733 (30 or 60 mg/kg) exhibited slightly stronger antitumor activities than the AT13387-alone group.

物理化学性质&存储条件

分子量 240.23
分子式 C10H6F2N2OS
外观性状 Solid
CAS No.
储存条件
固体粉末
-20°C 12 个月; 4°C 6 个月
配置液
-80°C 6 个月; -20°C 6 个月
Shipping
Solubility

10 mM in DMSO
Chemical Name/SMILES

5,7-Difluoro-2-imino-2H-chromene-3-carbothioamide

参考文献

1. Qiuyue Zhang, et al. J Med Chem. 2024 Aug 15. doi: 10.1021/acs.jmedchem.4c00722.

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