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.¹ 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.^1,2 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.^1,3 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.⁴ 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.

WARNING This product is not for human or veterinary use.

1. Zheng, X.L., Kitamoto, Y., and Sadler, J.E. Enteropeptidase, a type II transmembrane serine protease. Front. Biosci. (Elite Ed.) 1, 242-249 (2009).

2. Antalis, T.M., Buggee, T.H., and Wu, Q. Membrane-anchored serine proteases in health and disease. Proteases in Health and Disease 1-34 (2011).

3. Sadler, J.E. Enteropeptidase. Handbook of Proteolytic Enzymes 3, 2648-2653 (2013).

4. Yashiro, H., Hamagami, K., Hiyoshi, H., et al. SCO-792, an enteropeptidase inhibitor, improves disease status of diabetes and obesity in mice. Diabetes Obes. Metab. 21(10), 2228-2239 (2019).