Enterokinase Humaan

Source:Escherichia Coli.Physical Appearance:Liquid solution.Biological ActivitynullEnteropeptidase 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 (EC3.4.21.9) . Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.Enterokinase Human produced in E.Coli cells is a single, non-glycosylated polypeptide chain containing 237 amino acids (785-1019aa) and having a molecular mass of 26.4kDa. Enterokinase is purified by proprietary chromatographic techniques

Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, TMPRSS15, MGC133046, Transmembrane Protease Serine 15.

Greater than 85.0% as determined by SDS-PAGE.

Enterokinase 1mg/mL is supplied in 20mM Tris-HCl, pH 8.0, and 10% glycerol.

Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Avoid multiple freeze-thaw cycles.

MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH