Enterokinase from bovine intestine

Enterokinase also referred to as enteropeptidase, is a transmembrane protein. This intestinal protease contains a heavy chain and a light chain linked by a disulfide bond. The amino-terminal sequence of the bovine enteropeptidase is homologous to trypsin-like serine proteases.[1] 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.

Enterokinase from bovine intestine has been used to remove S-Tag and N-terminal His-tag from recombinant glutathione peroxidase 1 (Gpx1).[2] It has also been used to cleave interleukin-2 (IL-2) protein from the granules[3]

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.

Enterokinase catalyzes the proteolytic activation of pancreatic proteases. This action prevents the harmful tissue damage produced by the autoactivation of pancreatic proteases in the pancreas. Enterokinase recognizes Lys or Arg residues in the peptide. Lack of enterokinase can harm food digestion and absorption mechanism.[1] 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.[2]

Supplied with optimized enterokinase buffer

Do not used PVDF since free FLAG peptide will bind to the PVDF membrane.

One unit is that amount of enterokinase which results in >95% cleavage of 1 µg 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.