Enteropeptidase, EC 184.108.40.206, Enterokinase, Serine protease 7, ENTK, MGC133046.
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 Lieberk?hn, 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(EC220.127.116.11). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
Enterokinase Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids with a 6 × His at C-terminus and having a molecular mass of 28.0kDa.
The Enterokinase Bovine is purified by proprietary chromatographic techniques.
Sterile liquid solution.
Bovine EK is supplied in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
One year when stored at -20°C.
Please avoid freeze-thaw cycles.
One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.
Safety Data Sheet
ProSpec'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.