Recombinant Human Enteropeptidase - 20 IU
Introduction: 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 LieberkÃ¼hn, 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. 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.
Source: Escherichia Coli.
Physical Appearance: Liquid solution.
Formulation: 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
Stability: One year when stored at â€“20Â°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 4Â°C, in 16 hours at 25Â°C or in 8 hours at 37Â°C.
Assay Conditions: 50mM TRIS-HCl or sodium phosphate (pH 8.0) at 25Â°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, 500mM NaCl and 50% glycerol.
Usage: Celprogen'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.