Anti-Human CPM Antibody Pair

Product Description: Carboxypeptidase M (CPM) is a membrane-bound zinc metalloprotease that specifically removes C-terminal basic residues (arginine or lysine) from peptides and proteins. It is widely distributed in human tissues and plays important roles in regulating peptide hormone and growth factor activity at the cell surface. CPM consists of a 295-residue N-terminal catalytic domain and an 86-residue C-terminal domain, with a unique 25-residue C-terminal extension for GPI-anchor attachment. The enzyme is involved in various physiological processes, including inflammation, angiogenesis, and cell differentiation. CPM has been associated with several pathological conditions, such as renal cell carcinoma, where its expression is lost in tumor cells but abundant in tumor-associated foam cells. Additionally, CPM has been linked to silicosis susceptibility, with the rs12812500 variant potentially affecting CPM expression and increasing disease risk. Protein Function: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins [The Uniprot Consortium]