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Enteropeptidase/Enterokinase, Light Chain Human Recombinant ( Enterokinase Human )
DescriptionEnteropeptidase 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
Data sheet
| Formulation | 50mM Tris-HCl, pH 8.0, 0.5M NaCl, 1mM CaCl2 and 50% glycerol. |
| Purity | Greater than 95.0% as determined by HPLC-SEC. |
| 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. |
| Protein Background | 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 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. |
| Expression host | Escherichia Coli. |
| Synonyms | Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15. |
| Reagent Appearance | Liquid solution. |
| 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. |