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. Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.
Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids. A fully biologically active molecule, rbEK has a molecular mass of 22.7 kDa and is obtained by proprietary chromatographic techniques at GenScript.
Components:
100 IU(or 500IU or 5000IU) Recombinant Bovine Enterokinase (in 20mM Tris-HCl, pH 7.4, 200mM NaCl,
2mM CaCl 2, 50% glycerol)100µg Cleavage Control Protein (Lyophilized after extensive dialysis against PBS, pH 7.0)3.6 ml EK Dilution/Storage Buffer (20mM Tris-HCl, pH 7.4, 200mM NaCl, 2mM CaCl2, 50% glycerol)1.8 ml 10X EK Cleavage/Capture Buffer (200mM Tris-HCl, pH 7.4, 500mM NaCl, 20mM CaCl2)