Enteropeptidase or enterokinase is an enzyme involved 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 pancreatic digestive enzymes. Enteropeptidase is a serine protease enzyme (EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins. Porcine enteropeptidase is a specific protease which cleaves after the lysine at its recognition site: Asp- Asp-Asp-Asp-Lys. Enterokinase will not cleave a site followed by proline. If a fusion tag is located in the N-terminus with an enterokinase site, enterokinase will be able to remove the fusion tag and to generate the protein exactly as you need without adding any unwanted residues.
Source:Enterokinase, from porcine
Unit Definition:One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, 2mM CaCl2.
Storage and Stability:For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：100IU
Source Antigen：Porcine
Grade：Molecular Biology Grade
Form：Supplied as a liquid in 50mM Tris-HCl, pH 8.0, 0.5M sodium chloride, 50% glycerol.
