Human Carboxypeptidase M Alexa Fluor™ Plus 594-conjugated Antibody

Carboxypeptidase M (CPM) is a 50‑65 kDa monomer that belongs to the regulatory CPN/E subfamily, peptidase M14 family of enzymes. It is widely expressed, being found on macrophages, fibroblasts, endothelial cells, oligodendrocytes and Schwann cells, dendritic cells, osteoblasts and bronchial epithelium. Carboxypeptidase M is a GPI‑linked glycoprotein that is best known as a peptidase that cleaves basic amino acids (aa) from the carboxyterminal of a number of peptides, including EGF and bradykinin. It is also known to bind to apparent substrates and undergo a conformational change that links it with the kinin B1 GPCR, initiating signal transduction. Mature human Carboxypeptidase M is 406 aa in length (aa 18-423). It contains one large enzymatic region (aa 19-310) and two critical glutamic acid residues at Glu260 and Glu264. Like many GPI‑linked proteins, Carboxypeptidase M undergoes solubilization and is reportedly found in urine and amniotic fluid. Over aa 18-423 (mature Carboxypeptidase M), human Carboxypeptidase M shares 86% aa sequence identity with mouse Carboxypeptidase M.