English name: Enterokinase; Enteropeptidase
Other names: peptone intestinal enzyme; intestinal proteases; erepsin; intestinal enzyme activation
Molecular Weight: Approximately 43KDa, a single glycosylated polypeptide chain containing 235 amino acids.
Dynamic definition of: One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25 ℃ in a buffer containing 25mM Tris-HC1, pH7.6; 50mM NaC1 and 2mM Cac12
Formulation: 50mM Tris-HC1, pH8.0; 0.5mM NaC1 and 50% glycerol
Characters: sterile liquid recombinant
Usage: biochemical studies is a serine protease which can efficiently hydrolyze specific engineering bacteria fusion protein (recognition sequence is - (Asp) 4Lys ↓ -) releasing the target protein due Enterokinase highly specific. high hydrolysis efficiency, it is widely used in the development of genetic engineering products; it can be used as a protease specifically recognize and cleave the substrate containing enterokinase cleavage site, which is one of the application is as a tool for recombinant protease specific cleavage fusion proteins, pharmaceutical industry research and genetic engineering, biochemistry, molecular biology and other biological engineering especially for, but limited natural Enterokinase sources and extracted from animal tissue contaminated with other proteases enterokinase, which gives practical application difficult. This requires the use of genetic engineering process for producing high purity enterokinase. genetic engineering process for producing high-purity native enzyme enterokinase activity similar, but enterokinase cleavage rate faster
Save: -20 ℃