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.
Source:Recombinant protein corresponding to the catalytic subunit of bovine Enterokinase, expressed in Pichia pastoris and is purified to yield a high enzyme activity preparation.
Unit Definition:One unit of EK is the amount of enzyme required to digest 0.5mg of thioredoxin-NP-27 fusion protein to 90% completion in 16 hours at 37°C.
AA Sequence:EK recognizes the sequence Asp-Asp-Asp-Asp- Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this sequence.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store 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：20IU
Source Antigen：Recombinant, Pichia pastoris
Grade：Purified
Purity：Purified
Form：Supplied as a liquid in 50mM potassium phosphate, pH 8.0, 500mM sodium chloride, 50% glycerol.
