Catalogue Number | ENZ-260 |
Synonyms | Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15. |
Introduction | Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenums 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. |
Description | Enteropeptidase Human is a specific protease that cleaves after the sequence
Asp-Asp-Aps-Aps-Lys. The light chain of enteropeptidase has full enzymatic activity. No other protease activity was detected. Human enteropeptidase binds specifically to STI-agarose. The affinity puirifed Human Enterokinase contains amino acids from 785 to 1019. |
Source | Escherichia Coli. |
Physical Appearance | Liquid solution. |
Formulation | 50mM Tris-HCl, pH 8.0, 0.5M NaCl, 1mM CaCl2 and 50% glycerol. |
Stability | One year when stored at –20°C, three weeks at room temperature. |
Unit Defenition | One unit of human enteropeptidase will cleave 2 mg of thioredoxin/human EGF fusion protein with the Asp-Asp-Asp-Asp-Lys sequence at the joining point in 22 hours at 4°C, in 16 hours at 25°C or in 8 hours at 37°C. |
Assay Conditions | 50mM Tris-HCl or sodium phosphate (pH 8.0) at 25°C with or without CaCl2. The enzyme is active at a pH range of 6.0-9.0. |
Dilution buffer | 50mM Tris-Hcl, pH 8.0 at 25C, 500mM NaCl, 1mM CaCl2 and 50% glycerol. |
Purity | Greater than 98.0% as determined by SDS-PAGE. |
Usage | Prospecs 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. |