Recombinant Human Enteropeptidase/Enterokinase Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Enteropeptidase, also known as enterokinase, is a type II transmembrane serine protease that initiates activation of pancreatic proteases by converting trypsinogen to trypsin, which subsequently leads to activation of chymotrypsin, carboxypeptidases and elastases in the intestine (1). Located in the intestinal brush border, enteropeptidase is a disulfide bond-linked dimer of an N-terminal heavy chain (HC) and C-terminal light chain (LC) derived from the same single-chain precursor. The non-catalytic multidomain HC includes a short cytoplasmic tail, a transmembrane, a MSCR, a MAM, two CUB, and two LDL-receptor class A domains while the LC contains the catalytic domain of trypsin-like serine proteases (1,2). Enteropeptidase is known to have high sequence specificity making it useful as a biotechnological tool for recombinant fusion domains. Human enteropeptidase LC has greater efficiency and specificity than bovine enteropeptidase LC (3,4). Removal of HC domains results in significant loss of activity towards its physiological substrate trypsinogen (5-7) although cleavage of small peptidyl substrates remains equivalent (6,8). Enteropeptidase inhibition may be a target in diabetes and obesity (9,10). The purified activated recombinant human Enteropeptidase corresponds to the heterodimer of LC and HC without the transmembrane domain.

Array 10438-SE

• Enteropeptidase/Enterokinase Antibodies
• Enteropeptidase/Enterokinase Lysate
• Enteropeptidase/Enterokinase Proteins
• Enteropeptidase/Enterokinase Proteins and Enzymes