||Recombinant Bovine Enterokinase produced in E.coli is a single glycosylated polypeptide chain containing 235 amino acids and having a molecular mass of approximately28 kDa.
||Enterokinase is a serine proteinase in the duodenum that plays a critical role in mammalian digestion. 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.
||Approximately 28 kDa, a single non-glycosylated polypeptide chain containing 235 amino acids.
||≥ 2 x 104 units/mg recombinant enterokinase.
||One unit is defined as the amount of enzyme needed to cleave 50 ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25 mM Tris-HCl, pH 7.6, 50 mM NaCl, and 2 mM CaCl2.
||50 mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
||Less than 1EU/g of rbEK as determined by LAL method.
||One year when stored at -20°C. Avoid repeated freeze/thaw cycles.