Recombinant Human Aminopeptidase N/CD13 His Avi Protein, CF

Aminopeptidase N (APN) is a type II transmembrane zinc-dependent metalloprotease that is widely expressed in many cells, tissues, and species. APN forms an active homodimer where each monomer contains a short cytoplasmic tail, a transmembrane region, and an extracellular domain with a Ser/Thr rich region and a metalloprotease catalytic domain (1,2). APN is also known as leukocyte surface differentiation antigen CD13, microsomal aminopeptidase, alanyl aminopeptidase, and aminopeptidase M (1-3). The protein cleaves the N-terminal neutral amino acids from bioactive peptides like neuropeptides and immunomodulatory peptides including oxytocin, vasopressin, angiotensin III, and tuftsin resulting in their degradation or modulation (2,4). Consequently, APN is implicated to play many biological roles within the immune system, angiogenesis, mestastasis, and cancer (2). Both APN expression and activity are altered in cancer making it a marker and a pharmacological intervention target (5,6). It is targeted in CAR T therapies for cancers such as B-cell lymphoma and multiple myeloma (2,7). In addition, APN serves as a receptor for several human viruses such as coronavirus 229E (8) and human cytomegalovirus making it of interest as a target in these fields (9,10).