Description
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment.
Abbr
Enterokinase, Recombinant (Bovine)
Applications
Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. Enterokinase from bovine intestine has been used in a study to assess duodenase as a potential activator of cascade digestive proteases. Enterokinase from bovine intestine has also been used in a study to investigate an inhibitor of enteropeptidases and trypsin from the bovine duodenum. The enzyme from Creative Enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in Escherichia coli.
Package
vial of ~0.2 unit
Form
Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder.
Enzyme Commission Number
EC 3.4.21.9
Activity
Type I, > 20 units/mg protein
Molecular Weight
28 kDa light chain form
Concentration
> 0.1 mg/mL
Unit Definition
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25°C.
Function
scavenger receptor activity; serine-type endopeptidase activity
Synonyms
enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8
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