Anti-Aminopeptidase N/CD13 Antibody, clone BR2 clone BR2, from mouse

Aminopeptidase N (EC 3.4.11.2; UniProt P15144; also known as Alanyl aminopeptidase, Aminopeptidase M, AP-M, AP-N, CD13, gp150, hAPN, Microsomal aminopeptidase, Myeloid plasma membrane glycoprotein CD13) is encoded by the ANPEP (also known as APN, CD13, PEPN) gene (Gene ID 290) in human. Aminopeptidase N (CD13) is a 150-kDa membrane glycoprotein belonging to the superfamily of zinc metalloproteases. CD13 preferentially cleaves N-terminus neutral amino acids, most notably alanine residue, and is widely expressed as a homodimer of 280 kDa on the cell surface in many tissues, including intestinal epithelia and the nervous system. CD13 is involved in many physiological processes such as antigen presention regulation, differentiation, proliferation, apoptosis, chemotaxis, phagocytosis, pain sensation, adhesion, viral infection, cancer metastasis and angiogenesis. CD13 mediates its biological functions through its role as a receptor or co-receptor in cellular signaling, as well as via peptidase activity. CD13 is a receptor for human coronavirus (HCoV) and cytomegalovirus (HCMV), and many proteins are found in complex with CD13, including galectin-3, galectin-4, Grb2, IgG receptors (Fc Rs), reversion-inducing cysteine-rich protein with kazal motifs, Sos, and the pro-inflammatory cytokine 14-3-3 . Human CD13 consists of a short N-terminal cytoplasmic end (a.a. 2-8), a transmembrane domain (a.a. 9-32), and a large extracellular portion (a.a. 33-967) composed of a Ser/Thr-rich region (a.a. 33-68) and the metalloprotease domain (a.a. 69-967), including an HCoV-229E-interacting region (a.a. 26-353) and a Substrate-binding region (a.a. 352-356).