Enterokinase (EC 3.4.21.9) is a serine proteolytic enzyme, which can recognize the sequence of ASP ASP Lys (DDDDK) in protein efficiently and specifically, a hydrolyzed peptide that binds at the c-terminal end of lysine (Lys, K), producing cleavage, hydrolyzes trypsinogen to trypsin in the body.

Because enterokinase has high specificity and efficient enzymatic cleavage, it is widely used in genetic engineering. Product development. Natural enterokinase consists of a 115 kDa heavy chain and a 35 kDa light chain. The heavy chain anchors the cell membrane and the light chain has full enzymatic catalytic activity. The central region of light chain activity (235A. A., 26.2 kDa) secreted and expressed by E. coli is more active than that of bovine enterokinase, which is particularly suitable for enzymatic digestion of protein from the fusion of genetic engineering.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays the role of converting trypsinogen to its active form trypsin and indirectly activates pancreatic digestive enzymes. Enterokinase is a specific protease that is cleaved 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 proline. RBK has the highest activity than EK from other species and is used wildly in biochemical applications. rbEK with 6 x His-tag binds with Ni2 + affinity chromatography and was designed to remove it from the digestion system.

Recombinant bovine enterokinase (His-tagged) (rank) as a light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 x His at the C-terminus. RK, a fully biologically active molecule, has a molecular mass of 40 kDa and is obtained using proprietary GenScript chromatographic techniques.