2016
DOI: 10.15171/ijb.1331
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Soluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli

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Cited by 4 publications
(3 citation statements)
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“…Mis-pairing of disulfide bond in cysteines will cause mis-folding during protein synthesis and form the inclusion body. The inclusion body formation in recombinant proteins can result in inactive or non-functional proteins [14,15].…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Mis-pairing of disulfide bond in cysteines will cause mis-folding during protein synthesis and form the inclusion body. The inclusion body formation in recombinant proteins can result in inactive or non-functional proteins [14,15].…”
Section: Discussionmentioning
confidence: 99%
“…However, the refolding process may occur randomly which cause low-yield protein [16]. coli [15,17,20]. Fusion partner protein (His) 6tag helped us in the protein purification process.…”
Section: Discussionmentioning
confidence: 99%
“…Utilizing strong promoters as the routine approach in E. coli expression system is likely to produce great concentrations of desired proteins and formation of insoluble protein aggregates. Since the expression of protein in its soluble format is more desirable considering no need for further refolding steps different approaches have been applied to address this problem ( 26 ). Reducing rate of protein synthesis by decreased inducer concentration, induction at lower temperatures ( 27 ), medium optimization ( 28 ), co-expression of chaperons ( 29 ) and foldases ( 30 ) and the use of fusion tags ( 31 ) have been investigated in several studies.…”
Section: Introductionmentioning
confidence: 99%