Description
Product Characteristics: CD13 (aminopeptidase N, APN) is a 150 kDa type II transmembrane zinc-binding ectopeptidase expressed on various cell types. This metalloprotease preferentially catalyzes removal of neutral amino acids from small peptides, thus activating or inactivating bioactive peptides. CD13 has also role in extracellular matrix degradation, antigen processing and signal transduction, is important in inflammatory responses, regulates intercellular contact, cell motility and vascularization. CD13 is involved in protection of leukemic cells against apoptosis and its expression associated with poor prognosis of carcinomas.
Target Information: Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma. [provided by RefSeq, Jul 2008]