Enterokinase Human
Enteropeptidase/Enterokinase, Light Chain Human Recombinant

Synonyms:
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

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 Lieberkühn, 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.

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 –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, 500mM NaCl and 50% glycerol.

Usage:
Prospec'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.