epitope mapping within an internal region of Aminopeptidase P2 of human origin
recommended for detection of Aminopeptidase P2 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
Aminopeptidase P2 Background Information Aminopeptidases comprise a family of enzymatic proteins that are widely distributed in both eukaryotes and prokaryotes and function to catalyze the removal of amino acids from the N-termini of proteins. Aminopeptidase P2, also known as XPNPEP2 (X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound), is a 674 amino acid lipid-anchored cell membrane protein that belongs to the pita bread fold family of peptidase proteins. Expressed in colon, lung, kidney, heart, liver, placenta and small intestine, Aminopeptidase P2 exists as a homotrimer that functions as a metalloprotease and plays a role in Bradykinin metabolism, as well as in inflammatory responses throughout the body. Aminopeptidase P2 binds manganese as a cofactor and is subject to heavy post-translational glycosylation.
