A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg²⁺ or Mn²⁺-dependent (PPM) family, composed primarily of PP2C.

Source: The immunogen used to generate the purified antibody was a peptide conjugated to KLH corresponding to the sequence NH2-Thr-Pro-Pro-Arg-Gly-Met-Ile-Thr-Lys-Gln-Ala-Lys-Lys-COOH. This peptide antibody corresponds to C -terminal peptide of PP1 gamma 1 catalytic subunit having a MW of 37kD. The sequence used is amino acid 311-323.