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	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	biotechnology	EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation	683266	
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	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	synthesis	gene engineering studies on processing fusion proteins	667758	
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	
3.4.21.9	biotechnology	study presents a simple and cost-effective procedure for a large-scale production	684030	
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	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	additional information	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