Hepsin Products

Description

Hepsin, also known as TMPRSS1, is part of a family of type II transmembrane serine proteases (TTSPs) (1) that cleaves critical target proteins including Hepatocyte growth factor (HGF), uromodulin (UMOD), uPA, and macrophage-stimulating protein (MSP) at specific cleavage sites following basic residues with a strong preference for arginine residues (2-5). Hepsin is a 417 amino acid polypeptide that is activated to a two-chain disulfide-linked form. Hepsin, like other proteases in this family, contains an N-terminal cytoplasmic tail and transmembrane domain, and an extracellular stem region with an SRCR domain and C-terminal serine protease domain with a conserved activation site (1, 6). It is most highly expressed in liver, but is also present in many other tissues, notably lung, kidney, and skeletal muscle (7) and is found at high levels in several cancers including prostate, breast, and ovarian (2, 5, 8-10). In the liver, hepsin functions to regulate glucose, lipid, and protein metabolism through proteolytic conversion of pro-HGF to HGF, a potent ligand for Met signaling and dysregulation (11). Involvement in cancers has made hepsin a target of interest using either small molecule inhibitors or antibodies to neutralize their proteolytic activity, for example for prostate cancer and metastasis (12-14). Hepsin is also of interest for its potential role in osteoarthritis (15) and its ability to cleave surface proteins of respiratory viruses making it a therapeutic target for respiratory viral diseases (13). Recombinant Human Hepsin was expressed as a secreted, soluble protein lacking its cytosolic and transmembrane domains and activated. 

Bioinformatics

Uniprot	P05981.1
Product By Gene ID	3249
Alternate Names	EC 3.4.21 EC 3.4.21.106 Hepsin HPN serine protease hepsin catalytic chain serine protease hepsin TMPRSS1 TMPRSS1serine protease hepsin non-catalytic chain Transmembrane protease serine 1 transmembrane protease, serine 1