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Recombinant Bovine Enterokinase produced in Pichia. Pastoris is a single glycosylated polypeptide chain containing 235 amino acids and having a molecular mass of approximately 43.0 kDa.
Less than 1EU/mg of rbEK as determined by LAL method.
One year when stored at -20°C. Avoid repeated freeze/thaw cycles.
Crystal structure of Enteropeptidase with an inhibitor protease, serine, 7 (human)
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. More recently, the enterokinase has been shown to have a broad utility in cleaving fusion proteins produced in Escherichia coli. The enzyme is particularly suitable for this role because of its high degree of specificity, its tolerance to a wide range of reaction conditions, and the fact that its recognition sequence lies entirely on the aminoterminal side of the scissile bond. This enzymatic activity allows release of carboxyl-terminal fusion partners from fusion proteins without leaving unwanted amino acid residues on their amino termini.