Cat No.
NATE-0872
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 (Calf)
Source
Calf intestine
Species
Calf
Form
Lyophilized
Enzyme Commission Number
EC 3.4.21.9
Concentration
1:50 % (w/w)
Molecular Mass
150 kDa
Specificity
Serine protease acting as a restriction protease that recognizes the amino acid sequence -(Asp)4-Lys-X. The aspartic acid residues can be partially substituted by glutamic acid.
Optimum pH
8
Applications
Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. For the processing of recombinant proteins, the desired protein is fused with Enterokinase recognition sequence. After purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase.
Synonyms
enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase
