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. PTP inhibitor IV is an uncharged, 1,4-di-substituted, phenyl-linked bis-trifluoromethylsulfonamido phosphate mimetic that acts as a reversible, competitive, and active-site directed inhibitor of SHP-2, PTP1B, PTP-ε, PTP-Meg-2, PTP-σ, PTP-β, and PTP-μ (IC50s = 1.8, 2.5, 8.4, 13, 20, 6.4, and 6.7 μM, respectively).
