Enterokinase (Recombinant) is highly purified recombinant bovine enterokinase obtained from E. Coli. Enterokinase is highly specific serine protease that hydrolysis peptide bond at the carboxyl side of lysine residue preceded by four aspartic acids (FLAG-tag).
Enterokinase is used for removal of Flag-Tag from fusion proteins with the FLAG-tag.
- Animal free source of origin, therefore no any other contaminating proteases.
- Highly purified recombinant enterokinase that cleaves specifically after lysine preceded by four aspartic acid residues.
- Source: E. coli
- MW: 25.85 kDa
- Specific activity: One unit is defined as the amount of enzyme required to cleave 0.5 mg fusion protein to 95 % completion in 12-16 hrs at 25°C in 25 mM Tris-HCl, 1 mM CaCl2, pH:8.0.
- Storage:-20°C or below. Avoid repeated thawing. Prefereably, aliquot in small one time use aliquots before storing at -20°C or -70°C.
- Enterokinase is used for removal of Flag-Tag from fusion proteins with the FLAG-tag.
|Material Safety Data Sheet|
|Enterokinase (Recombinant)||20 U||
|Enterokinase (Recombinant)||100 U||
|Enterokinase (Recombinant)||5 x 100 U||