|Product Overview :
||Recombinant bovine TMPRSS15 protein (801-1,035) with a C-termina His-tag enterokinase was expressed in yeast.
||Enteropeptidase is a membrane-bound serine protease that converts the inactive enzyme trypsinogen to the active form trypsin, a protease that catalyzes the digestion of proteins in the gut. It is composed of an N-terminal domain with a transmembrane segment that anchors enteropeptidase to the cell membrane and an extracellular C-terminal protease domain that contains the activation cleavage site for enteropeptidase activity and a catalytic aspartic acid-histidine-serine triad. It is synthesized in the endoplasmic reticulum as a zymogen and transported to the brush border membrane of duodenal and jejunal enterocytes. Enteropeptidase activation occurs in a calcium- and pH-dependent manner and, upon activation, cleaves the Asp-Asp-Asp-Asp-Lys activation peptide on trypsinogen to produce trypsin. Pharmacological inhibition of enteropeptidase activity decreases food intake, body weight gain, and liver triglyceride and total cholesterol levels in diet-induced obese mice and diabetic obese ob/ob mice.
||Lyophilized from sterile 10 mM Tris-HCl, pH 7.2, with 2 mM calcium chloride, 100 mM sodium chloride, and 50% glycerol
|Molecular Mass :
|Protein length :
||≥95% estimated by SDS-PAGE
||≥ 1 year
||Store at -80 centigrade
|SDS-PAGE Analysis of Enteropeptidase :
Lane 1: MW Markers, Lane 2: Enteropeptidase, SDS-PAGE Analysis of Enteropeptidase. This protein has a calculated molecular weight of 27.1 kDa. It has an apparent molecular weight of approximately 44 kDa by SDS-PAGE under reducing conditions due to glycosylation.