|Detection of Human Lysosomal Pro‑X Carboxypeptidase/PRCP by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Lysosomal Pro‑X Carboxypeptidase/PRCP Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7164) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Lysosomal Pro‑X Carboxypeptidase/PRCP at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
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.
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