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Status |
Public on Nov 24, 2010 |
Title |
Role of chaperones and a cytoplasmatic protease in recombinant protein production in E. coli at suboptimal growth temperature |
Organism |
Escherichia coli |
Experiment type |
Expression profiling by array
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Summary |
Recent studies have revealed that at lower cultivation temperatures (25°C) much higher percentage of correctly folded recombinant proteins can be extracted from inclusion bodies. The goal of our research was to investigate mechanisms determining characteristics of non-classical inclusion bodies production using gene expression profiling. Two strains of recombinant E. coli [BL21 (DE3)] grown at three different temperatures (25°C, 37°C and 42°C) were included in experiment.
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Overall design |
Gene expression was studied in two recombinant strains (production and control strain), grown at three different temperatures (25, 37 and 42 oC) in three biological replicates. Cells were harvesed at OD=4, except for the cells grown at 25 oC, here they were harvested at OD=4 and OD=10.
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Contributor(s) |
Mahnič M, Baebler S, Blejec A |
Citation(s) |
24061173 |
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Submission date |
Nov 23, 2010 |
Last update date |
Nov 07, 2014 |
Contact name |
Spela Baebler |
E-mail(s) |
spela.baebler@nib.si
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Organization name |
National Institute of Biology
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Department |
Department of Biotechnology and Systems Biology
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Street address |
Vecna pot 111
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City |
Ljubljana |
ZIP/Postal code |
1000 |
Country |
Slovenia |
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Platforms (1) |
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Samples (23)
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Relations |
BioProject |
PRJNA134285 |