Description_x000D_ General description_x000D_ Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG._x000D_ Application_x000D_ Conformation of FLAG peptide removal can be determinied by dot blot assay and SDS-PAGE analysis using nitrocellulose._x000D_ Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags._x000D_ Removes FLAG peptide from N-terminal and Met-N-terminal fusion proteins._x000D_ Packaging_x000D_ Supplied with optimized enterokinase buffer_x000D_ Unit Definition_x000D_ One unit is that amount of enterokinase which results in >95% cleavage of 1 mg of purified FLAG-BAP fusion protein in 18 hours at 37 °C. One FLAG-BAP unit is equal to 10x the activity of a standard trypsinogen unit._x000D_ Other Notes_x000D_ Do not used PVDF since free FLAG peptide will bind to the PVDF membrane.