Human Lysosomal Pro-X Carboxypeptidase/PRCP Antibody

PRCP (Prolylcarboxypeptidase; also PCP, lysosomal Pro-X carboxypeptidase and lysosomal carboxypeptidase C) is a lysosomal 57-62 kDa glycoprotein member of the S28 family of proteases. It is expressed by a number of cells including fibroblasts, macrophages, and endothelial cells. PRCP cleaves a variety of single C‑terminal amino acids (aa) adjacent to a Pro residue and is known to act on, and inactivate, peptides such as prekallikrein, alpha-MSH and angiotensin II plus III. Human PRCP is apparently synthesized as a prepropeptide that contains a signal sequence (aa 1-21), a short prosequence (aa 22-45) and a 451 aa mature region (aa 46-496). The mature region demonstrates a Ser-carboxypeptidase domain (aa 55-477) that, in itself, possesses an SKS domain that caps the enzyme's catalytic site. The molecule is known to be mannosylated and to form noncovalent homodimers. There is one splice variant that contains a 21 aa insertion after Lys56. Over aa 1-496, human and mouse PRCP share 77% aa sequence identity.