EC Number   |
Application |
Reference |
|---|
   3.4.21.9 | analysis |
cellular libraries of peptide substrates, CLiPS, are used to study substrate specificities, fluorescent reporter substrates on the surface of Escherichia coli as N-terminal conjugates are used as whole-cell protease activity assays |
684000 |
| 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 | biotechnology |
enteropeptidase is a serine protease used in different biotechnological applications. For many applications the smaller light chain can be used to avoid the expression of the rather large holoenzyme |
718352 |
| 3.4.21.9 | biotechnology |
purification of 6.8 mg bioactive enzyme from 1l fermentation broth |
683994 |
| 3.4.21.9 | biotechnology |
study presents a simple and cost-effective procedure for a large-scale production |
684030 |
| 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 | 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 | 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 |
