Enterokinase is a highly specific mammalian serine protease that recognizes the amino acid sequence Asp-Asp-Asp-Asp-Lys（DDDDK） and hydrolyzes peptide link of C terminal from Lys, tansfer trypsinogen into trypsin.
Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible Enterokinase recognition site for removal of affinity tags. Cleavage is done either before or after fusion protein purification.
Enterokinase Removal Kit is excellent tool for the excision of bovine enterokinase from mixtures containing a fusion protein cleaved by the enzyme. Using the kit, removal of essentially all enterokinase (as judged by antigenic or enzymatic activity assays) is accomplished by binding with immobilized rabbit antibodies to calf intestine enterokinase followed by spin filtration. The protein of interest remains in the filtrate. Enterokinase, its fragments and aggregates as well as some contaminating proteins are depleted from the cleavage mixtures regardless of their enzymatic activity.
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