||Enhanced recombinant enterokinase light chain with 6 histidines expressed from modified human kidney cell line. Enterokinase (EK) is a specific protease that cleaves a protein after lysine residue at its recognition site: Asp-Asp-Asp-Asp-Lys. Enterokinase will not work if the recognition site is followed by proline. The rEKLx6 contains 6X His tags and can be removed from the cleavage reaction mixture by filtering through Nickel Cadmium column.
||Enterokinase is a serine proteinase in the duodenum that plays a critical role in mammalian digestion. It is the physiological activator of pancreatic trypsinogen. It converts trypsinogen into its active form trypsin, by cleaving its aminoterminal hexapeptide Val(Asp)4-Lys.
||< 1.0 EU per 1 microgram of protein (determined by LAL method)
||Approximately > 50 Unit/mg. One unit will hydrolyze 1 umole of p-nitroaniline per minute at pH 8.0 at 37°C using 1mM of Gly-Pro p-nitroanilde as a substrate.
||In 20 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 8.0 (10% glycerol)
||Store at 4°C for 1-2 weeks. For long term storage store at -20°C or -80°C. Aliquot to avoid repeated freezing and thawing.