|Synonyms||Enteropeptidase, ENTK, PRSS7|
|Description||Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.
Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.
|Biological Activity||100 IU/μg|
|Measured Molecular Weight||40 kDa, observed by reducing SDS-PAGE.|
|Purity||> 95% as analyzed by SDS-PAGE.|
|Formulation||Lyophilized from a 0.2 μm filtered solution in 20mM Tris-HCl, pH 7.4, 200mM NaCl, 2mM CaCl2.|
|Reconstitution||Reconstitute lyophilized EK powder in sterile deionized water at 1mg/ml, then dilute in EK Dilution/Storage Buffer according to your requirement.|
|Endotoxin Level||<0.2 EU/μg, determined by LAL method.|
|Storage||Lyophilized recombinant Bovine Enterokinase (His-tagged) (rbEK) remains stable up to one year at -20°C from date of receipt. Please avoid freeze-thaw cycles.|
|Note||For research use only|
For more documents, please visit "Technical Support".