Description
Recombinant Enterokinase is a kind of highly purified recombinant bovine enterokinase. The enzyme has been extensively purified and there are no traces of other contaminating proteases. Enterokinase specifically hydrolyzes peptide bond at the carboxyl side of lysine residue preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys (DDDDK). So, Enterokinase can remove N-terminal fusion protein or tags to get aim protein with native amino acids sequence.Protease that cleaves specifically after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys (DDDDK).No any other contaminated proteases, no non-specific cutting sites. One unit is defined as the amount of enzyme needed to cleave 0.5mg of fusion protein in 12 to16 hours to get 95% completion at 25°C in 25mMTris-HCl,pH 8.0. Substrate: a special fusion protein