EC Number   |
Application |
Reference |
|---|
   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 | molecular biology |
the enzyme is used for cleavage of the N-terminal part of recombinant human interferon-alpha2a (IFN-alpha2a) and IFN-alpha2b, expressed in Escherichia coli strains strains BL21 and BL21 (DE3), for production of the protein without the N-terminal methionine residue |
718100 |
| 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 | molecular biology |
the high degree of specificity exhibited by enteropeptidase makes it a suitable reagent for cleaving recombinant proteins to remove affinity or other tags. However often unwanted cleavages elsewhere in the protein occur during cleavage of fusions when high amount of enzyme is required |
718359 |
| 3.4.21.9 | molecular biology |
the high specificity of the target site makes enterokinase an ideal tool for cleaving fusion proteins at defined cleavage sites |
717891 |
| 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 |
| 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 |
