Enterokinase Human
Greater than 85.0% as determined by SDS-PAGE.
Description
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
Product Specs
MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH
Product Science Overview
Enteropeptidase, also known as enterokinase, is a serine protease enzyme that plays a crucial role in the digestive process. It is responsible for the activation of pancreatic proteases by converting trypsinogen into trypsin, which subsequently activates other digestive enzymes such as chymotrypsin, carboxypeptidases, and elastases . The enzyme is highly specific for the cleavage sequence Asp-Asp-Asp-Asp-Lys (D4K), making it a valuable tool in biotechnology for the separation of recombinant protein fusion domains .
Enteropeptidase is a type II transmembrane serine protease composed of a heavy chain and a light chain. The light chain, which is the proteolytically active component, exhibits high substrate specificity . The human enteropeptidase light chain (hEPL) has been bioengineered to improve its utility in processing fusion proteins. Variants such as R96Q and Y174R have been created to enhance substrate specificity and enzymatic activity .
Recombinant human enteropeptidase light chain (rhEPL) is produced using various expression systems, including Pichia pastoris. This yeast expression system allows for the secretion of active enzymes with high yields. The recombinant enzyme retains full enzymatic activity and specificity, making it suitable for industrial and research applications .
The high specificity of enteropeptidase for the D4K sequence makes it an essential tool in molecular biology and biotechnology. It is used to cleave fusion proteins at specific sites, allowing for the separation and purification of target proteins. This is particularly useful in the production of therapeutic proteins and other recombinant products .
