Synonyms Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Introduction Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberkühn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
Description Enterokinase (rEK) Bovine Recombinant is the catalytic subunit of bovine enterokinase, which is expressed by the yeast and purified to yield a high enzyme activity preparation. EK recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this sequence.
Source Pichia pastoris
Physical Appearance Liquid solution.
Formulation EK in 50mM potassium phosphate, pH 8.0, 500mM NaCl and 50% glycerol should be stored at -20°C.
Stability One year when stored at –20°C, three weeks at room temperature.
Please avoid freeze-thaw cycles.
Unit Defenition One unit of EK is the amount of enzyme required to digest 0.5mg of thioredoxin-NP-27 fusion protein to 90% completion in 16 hours at 37oC.
Usage CHI's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.