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.
该Anti-Human Enteropeptidase的详细信息查看ReliaTech提供的产品说明书。溶解建议:Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml.