Phosphorylation and dephosphorylation on serine and threonine residues is critical for signal transduction and the regulation of numerous cellular functions. Phosphorylation levels are modulated by protein kinases and phosphatases. The Ser/Thr phosphatase PP5 (also known as PPT) is a model protein of the fourth subfamily of the PPP-family of phosphatases which includes PP1, PP2A, and PP2B. PP5 is primarily located in the nucleus, demonstrates widespread tissue distribution, and is highly conserved among species. It consists of a C-terminal catalytic domain and an N-terminal TPR (tetratricopeptide repeat) domain which is involved in protein-protein interactions. The TPRs of PP5 mediate protein phosphatase activity. TPRs mediate the interaction of PP5 with various proteins including the hsp90-glucocorticoid receptor complex and the kinase domain of ANP-guanylate cyclase receptor. PP5 is thought to be important in cell growth. For example, it functions upstream of p53 to regulate p21/WAF1/Cip1-mediated G1 growth arrest. Thus, PP5 is a nuclear protein phosphatase that is involved in signaling pathways of cell growth and arrest.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.