Enteropeptidase/Enterokinase initiates activation of pancreatic proteases by converting trypsinogen to trypsin, which in turn activates chymotrypsin, carboxypeptidases and elastases. Located in intestinal brush border, it is a disulfide bond linked dimer of the heavy and light chains, which are derived from the same single-chain precursor. The multi-domain-containing the heavy chain consists of a short cytoplasmic tail, a transmembrane, a SEA, a SRCR, a MAM, two CUB and two LDL-receptor class A domains. The light chain contains the catalytic domain of trypsin-like serine proteases.
該Anti-Human Enteropeptidase的詳細(xì)信息查看ReliaTech提供的產(chǎn)品說(shuō)明書(shū)。溶解建議:Centrifuge vial prior to opening. Reconstitute the antibody with 500 μl sterile PBS and the final concentration is 200 μg/ml.