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

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.

Enterokinase (rEK) Bovine Recombinant is the catalytic subunit of bovine enterokinase, which is expressed by the yeast and purified to yield a high enzyme activity preparation. 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.
Recombinant Bovine Enterokinase is a single glycosylated polypeptide chain containing 235 amino acids and having an MW of ~43kDa.

Pichia pastoris.

Sterile liquid solution.

Bovine EK in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.

One year when stored at –20°C.
Please avoid freeze-thaw cycles.

Greater than 95.0% as determined by SDS-PAGE.

One unit is defined as the amount of enzyme needed to cleave 50μg of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.

Each reaction contains 50 μg of partially purified thioredoxin-NP-27 fusion protein and varying amounts of Bovine EK. Reactions were incubated at 25°C for 16 hours and analyzed on a Coomassiestained 15% SDS gel.

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.