CPVL Protein, Human (HEK293, His)

The CPVL protein, a serine carboxypeptidase, may be involved in the digestion of phagocytic granules in lysosomes, in the inflammatory protease cascade, and in the pruning of peptides for antigen presentation. Carboxypeptidases are a large family of proteases that cleave individual amino acids from the carboxyl terminus of proteins or peptides. The functions of these enzymes include the degradation of phagocytic and/or endocytosed proteins in lysosomes and the digestive breakdown of proteins in the intestine. In addition to their degradative functions in the intestine, carboxypeptidases can activate or inactivate bioactive peptides such as angiotensin, bradykinin, and endothelin I. CPVL protein expression is induced during the maturation of monocytes into macrophages. In macrophages, possible functions of CPVL include digestion of phagocytic granules in lysosomes, participation in inflammatory protease cascades, and pruning of peptides for antigen presentation. Studies have found that the expression of CPVL protein is significantly up-regulated in both neovascular AMD (nAMD) and dry AMD, making it a potential biomarker for identification of AMD. Furthermore, high CPVL expression was associated with advanced clinical grade and poor prognosis. CPVL silencing activates the IFN-γ/STAT1 signaling pathway, thereby promoting glioma cell apoptosis and inhibiting cell proliferation and tumorigenicity in vitro and in vivo.