Enteropeptidase (bovine, recombinant)

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. Cayman's Enteropeptidase (bovine, recombinant) protein consists of 241 amino acids and has a calculated molecular weight of 27.1 kDa. By SDS-PAGE, under reducing conditions, the molecular weight of the protein is approximately 44 kDa due to glycosylation.Synonyms: Enterokinase, Serine Protease 7, Transmembrane Protease Serine 15. Purity: >95% estimated by SDS-PAGE. Source: Recombinant bovine C-terminal His-tagged enterokinase expressed in yeast. Amino Acids: 801-1,035. MW: 27.1 kDa. Formulation: (Request formulation change), Lyophilized from sterile 10 mM Tris-HCl, pH 7.2, with 2 mM calcium chloride, 100 mM sodium chloride, and 50% glycerol. UniProt Accession #: P98072-1.