EC Number   |
Application |
Reference |
|---|
   3.4.21.9 | more |
utility of enterokinase light chain as a site-specific cleavage enzyme is hampered by sporadic cleavage at other sites than the canonical D4K recognition sequence |
717409 |
| 3.4.21.9 | synthesis |
a huge number of therapeutic proteins such as antibodies, coagulation factors, growth hormones or vaccines are produced as fusion proteins. To obtain the therapeutic protein in its monomeric, active form, the fusion partner has to be removed either by chemical or enzymatic cleavage. Enterokinase is a very attractive tool for the in vitro cleavage of fusion proteins |
707812 |
| 3.4.21.9 | synthesis |
gene engineering studies on processing fusion proteins |
667758 |
| 3.4.21.9 | synthesis |
the cleavage immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence allows regeneration of native amino-terminal residues of recombinant proteins, e.g. removal of the thioredoxin and polyhistidine fusion partners from proteins of intrest |
95583 |
| 3.4.21.9 | synthesis |
the enzyme can be used for cleavage of fusion proteins due to its high specific activity |
653769 |
| 3.4.21.9 | synthesis |
the enzyme may be useful in amino acid sequence studies for the production of large fragents. The enzyme may also be useful in DNA-recombinant studies in releasing the desired polypeptide chain from neighboring sequences |
95569 |
| 3.4.21.9 | synthesis |
tool protease in the research and production of gene engineering |
667026 |
| 3.4.21.9 | synthesis |
useful tool for in vitro cleavage of fusion proteins |
653747 |
