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Stafib-1 Sale

目录号 : GC62254

Stafib-1 是首个选择性的 STAT5b SH2 结构域的抑制剂,其 Ki 值为 44 nM,IC50 值为 154 nM。

Stafib-1 Chemical Structure

Cas No.:1688703-26-5

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5 mg
¥1,980.00
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产品描述

Stafib-1 is the first selective inhibitor of the STAT5b SH2 domain, with a Ki of 44 nM and an IC50 of 154 nM[1].

Stafib-1 is the first small molecule which inhibits the STAT5b SH2 domain with more than 50-fold selectivity over STAT5a[1].

[1]. Nagarajan Elumalai, et al. Rational development of Stafib-2: a selective, nanomolar inhibitor of the transcription factor STAT5b. Sci Rep. 2017 Apr 11;7(1):819.

Chemical Properties

Cas No. 1688703-26-5 SDF
分子式 C26H24N2O11P2 分子量 602.42
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1 mM 1.66 mL 8.2999 mL 16.5997 mL
5 mM 0.332 mL 1.66 mL 3.3199 mL
10 mM 0.166 mL 0.83 mL 1.66 mL
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Research Update

Rational development of Stafib-2: a selective, nanomolar inhibitor of the transcription factor STAT5b

Sci Rep 2017 Apr 11;7(1):819.PMID:28400581DOI:10.1038/s41598-017-00920-3.

The transcription factor STAT5b is a target for tumour therapy. We recently reported catechol bisphosphate and derivatives such as Stafib-1 as the first selective inhibitors of the STAT5b SH2 domain. Here, we demonstrate STAT5b binding of catechol bisphosphate by solid-state nuclear magnetic resonance, and report on rational optimization of Stafib-1 (Ki = 44 nM) to Stafib-2 (Ki = 9 nM). The binding site of Stafib-2 was validated using combined isothermal titration calorimetry (ITC) and protein point mutant analysis, representing the first time that functional comparison of wild-type versus mutant protein by ITC has been used to characterize the binding site of a small-molecule ligand of a STAT protein with amino acid resolution. The prodrug Pomstafib-2 selectively inhibits tyrosine phosphorylation of STAT5b in human leukaemia cells and induces apoptosis in a STAT5-dependent manner. We propose Pomstafib-2, which currently represents the most active, selective inhibitor of STAT5b activation available, as a chemical tool for addressing the fundamental question of which roles the different STAT5 proteins play in various cell processes.

Halogen-substituted catechol bisphosphates are potent and selective inhibitors of the transcription factor STAT5b

Bioorg Med Chem 2017 Jul 15;25(14):3871-3882.PMID:28559059DOI:10.1016/j.bmc.2017.05.039.

The transcription factor STAT5b is an antitumor target. Recently, we presented the small molecules Stafib-1 and Stafib-2 as potent, selective inhibitors of the STAT5b SH2 domain. Here we report that halogen substitutions on the terminal phenyl ring of Stafib-1 and a close derivative are tolerated and specificity over the STAT5a SH2 domain is maintained, albeit with a slight reduction in activity. Our data demonstrate that the synthetic methodology used for generating Stafib-1 and Stafib-2 can be utilized to synthesize a small library of halogen-substituted derivatives, and extend the panel of catechol bisphosphate-based submicromolar and selective STAT5b inhibitors.

Nanomolar inhibitors of the transcription factor STAT5b with high selectivity over STAT5a

Angew Chem Int Ed Engl 2015 Apr 13;54(16):4758-63.PMID:25702814DOI:10.1002/anie.201410672.

Src homology 2 (SH2) domains play a central role in signal transduction. Although many SH2 domains have been validated as drug targets, their structural similarity makes development of specific inhibitors difficult. The cancer-relevant transcription factors STAT5a and STAT5b are particularly challenging small-molecule targets because their SH2 domains are 93% identical on the amino acid level. Here we present the natural product-inspired development of the low-nanomolar inhibitor Stafib-1, as the first small molecule which inhibits the STAT5b SH2 domain (K(i)=44 nM) with more than 50-fold selectivity over STAT5a. The binding site of the core moiety of Stafib-1 was validated by functional analysis of point mutants. A prodrug of Stafib-1 was shown to inhibit STAT5b with high selectivity over STAT5a in tumor cells. Stafib-1 provides the first demonstration that naturally occurring SH2 domains with more than 90% sequence identity can be selectively targeted with small organic molecules.