Formulation: Lyophilized from sterile 10 mM Tris-HCl, pH 7.2, with 2 mM calcium chloride, 100 mM sodium chloride, and 50% glycerol
Purity: ≥95% estimated by SDS-PAGE
Shelf life (days): 365
Notes: 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.{53814} 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.{53814,53815} 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.{53814,53816} 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.{53817} 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.
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