EC Number   |
Application |
Reference  |
|---|
   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 |
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 |
useful tool for in vitro cleavage of fusion proteins |
653747 |
| 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 |
tool protease in the research and production of gene engineering |
667026 |
| 3.4.21.9 | synthesis |
gene engineering studies on processing fusion proteins |
667758 |
| 3.4.21.9 | analysis |
enteropeptidase activity is influenced by accessibility of the target site and by downstream sequences |
683192 |
| 3.4.21.9 | biotechnology |
EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation |
683266 |
| 3.4.21.9 | medicine |
human TRAIL is a candidate for clinical application in cancer therapy, activity is lost in some forms of recombinant TRAIL, refolding of thioredoxin/TRAIL and cleavage by enteropeptidase yield a biological active anticancer agent |
683279 |
| 3.4.21.9 | biotechnology |
purification of 6.8 mg bioactive enzyme from 1l fermentation broth |
683994 |
