Protein tyrosine phosphatases (PTPs) remove phosphate from tyrosine residues of cellular proteins. Reversible phosphorylation catalyzed by the coordinated actions of protein tyrosine kinases and phosphatases is key to the regulation of the signaling events that control cell growth and proliferation, differentiation, and survival or apoptosis, as well as adhesion and motility. RK-682, a bioactive compound originally isolated from the fermentation of Streptomyces sp. 88-682, is an inhibitor of the PTPs.¹ It inhibits the phosphorylation of CD45 and VHR with IC₅₀ values of 54 and 2 µM, respectively, and arrests cell cycle progress at the G₁/S transition.¹ It is also reported to inhibit heparanase (IC₅₀ = 17 µM), an endo-β-D-glucuronidase involved in tumor cell invasion and angiogenesis.² RK-682 (calcium salt) is a less soluble version of the free acid.³

≥95%

Store at -20℃

1.Hamaguchi, T.,Sudo, T. and Osada, H. RK-682, a potent inhibitor of tyrosine phosphatase, arrested the mammalian cell cycle progression at G1phase. FEBS Letters 372(1), 54-58 (1995).

2.Ishida, K.,Hirai, G.,Murakami, K., et al. Structure-based design of a selective heparanase inhibitor as an antimetastatic agent. Molecular Cancer Therapeutics 3(9), 1069-1077 (2004).

3.Sodeoka, M.,Sampe, R.,Kojima, S., et al. Asymmetric synthesis of a 3-acyltetronic acid derivative, RK-682, and formation of its calcium salt during silica gel column chromatography. Chem.Pharm.Bull.(Tokyo) 49(2), 206-212 (2001).