2003
DOI: 10.1016/s1046-5928(03)00134-7
|View full text |Cite
|
Sign up to set email alerts
|

Production and purification of refolded recombinant human IL-7 from inclusion bodies

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
15
0
1

Year Published

2008
2008
2019
2019

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 30 publications
(16 citation statements)
references
References 26 publications
0
15
0
1
Order By: Relevance
“…Finally, when captured in inclusion bodies, the recombinant protein is considered to be protected against proteases [26,150,165]. Consequently, this strategy has been applied in numerous examples [6,79,87,122,164]. Main drawbacks remain the absence of generally applicable and inexpensive methods to refold the protein and the low overall yields of downstream processing [150].…”
Section: Optimization Of Inclusion Body Formationmentioning
confidence: 99%
“…Finally, when captured in inclusion bodies, the recombinant protein is considered to be protected against proteases [26,150,165]. Consequently, this strategy has been applied in numerous examples [6,79,87,122,164]. Main drawbacks remain the absence of generally applicable and inexpensive methods to refold the protein and the low overall yields of downstream processing [150].…”
Section: Optimization Of Inclusion Body Formationmentioning
confidence: 99%
“…In this work, the high recovery yield of soluble hIL-7 protein using affinity chromatography from fusion partner was strongly favored over literature reports where its retrieval from inclusion bodies resulted in a poor yield in the range of 5-10 mg/L (Ouellette et al 2003). Moreover, this strategy is expected to result in an authentic N-terminus of the fusion partner due to the high sequence specificity of SUMO protease (Butt et al 2005).…”
Section: Discussionmentioning
confidence: 99%
“…The expression level in E. coli hosts was uniformly poor in the range of 5-79 mg/L (Wickham and Walsh 2007;Zaremba-Czogalla et al 2015). The maximum hIL-7 expression achieved even in the bioreactor (720 L) was at a level of 10 mg/L after optimization of batch fermentation conditions (Ouellette et al 2003).…”
Section: Introductionmentioning
confidence: 97%
“…[11,12], several expression systems have been developed to produce recombinant rhIL-7. Currently, rhIL-7 is mainly produced in Escherichia coli expression system, which involves accumulation in inclusion bodies [13,14]. Although high expression levels are obtained in the bacterium, purification from inclusion bodies is usually quite difficult and leads to poor yields of refolded bioactive pharmaceutical ingredient.…”
Section: Introductionmentioning
confidence: 99%