Reconstitute lyophilized EK powder in sterile deionized water at 1mg/ml, then dilute in EK Dilution/Storage Buffer according to your requirement.
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 to be removed 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.
A fusion tag, called DYKDDDDK and consisting of eight amino acids (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys) including an enterokinase-cleavage site, was specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody, denoted as M1, binds the peptide in the presence of bivalent metal cations, preferably Ca2+. Elution is effected by chelating agents. Another strategy is competitive elution with excess of free DYKDDDDK peptide.
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