PTP1B (human, recombinant)

Protein tyrosine phosphatase (PTPs) are an enzyme superfamily that includes about 100 human proteins.¹ Their function is to remove phosphate from tyrosine residues of cellular proteins.² Reversible phosphorylation catalyzed by the coordinated actions of protein tyrosine kinases and phosphatases is of paramount importance to the regulation of the signaling events that underlie such fundamental processes as growth and proliferation, differentiation, and survival or apoptosis, as well as adhesion and motility.³ One of the most heavily studied PTP proteins is PTP1B. Data suggests PTP1B is a negative regulator in both insulin and leptin signaling.³ As such, PTP1B has become a leading diabetes drug target.¹

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1. Bishop, A.C., Zhang, X.Y., and Lone, A.M. Generation of inhibitor-sensitive protein tyrosine phosphatases via active-site mutations. Methods 42(3), 278-288 (2007).

2. Peters, G.H., Branner, S., Moller, K.B., et al. Enzyme kinetic characterization of protein tyrosine phosphatases. Biochimie 85(5), 527-534 (2003).

3. Zhang, S., and Zhang, Z.Y. PTP1B as a drug target: Recent developments in PTP1B inhibitor discovery. Drug Discov. Today 12(9-10), 373-381 (2007).