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Phosphatase inhibitors act on protein, lipid and inositol phosphatases that hydrolyze phosphate esters. A 2004 survey of the human genome counted 107 genes for protein tyrosine phosphatases (PTPs). Serine/threonine phosphatases such as protein phosphatases 1 and 2A (PP1, PP2A) reverse many kinase-driven signals. Calyculin A, reported in 1989 as an inhibitor of protein phosphatase activity, blocks both PP1 and PP2A. LB-100 targets PP2A, tautomycetin prefers PP1, and sodium orthovanadate inhibits PTPs broadly and is a common lysis buffer additive. Among lipid and inositol phosphatases, 3AC inhibits Src homology 2 (SH2) domain-containing inositol 5-phosphatase 1 (SHIP1), and L-690330 targets inositol monophosphatase.
