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, Native (Bovine)
Applications
Conformation of FLAG peptide removal can be determinied by dot blot assay and SDS-PAGE analysis using nitrocellulose. 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. Removes FLAG peptide from N-terminal and Met-N-terminal fusion proteins.
Product Overview
Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG.
Enzyme Commission Number
EC 3.4.21.9
Activity
Type I, > 20 units/mg protein
Molecular Weight
150 kDa (consisting of 115kDa and 35kDa subunits.)
Function
scavenger receptor activity; serine-type endopeptidase activity
Synonyms
enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8
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