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Items: 3

1.

Role of chaperones and a cytoplasmatic protease in recombinant protein production in E. coli at suboptimal growth temperature

(Submitter supplied) 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.
Organism:
Escherichia coli
Type:
Expression profiling by array
Platform:
GPL11242
23 Samples
Download data: TXT
Series
Accession:
GSE25561
ID:
200025561
2.

E.coli_12k_Combimatrix

(Submitter supplied) Probes are directly synthesized on a 12k Combimatrix array by an in situ oligo synthesis system developed by Combimatrix Corporation (Mukilteo, USA) using the Combimatrix CustomArray synthesizer.
Organism:
Escherichia coli
1 Series
23 Samples
Download data
Platform
Accession:
GPL11242
ID:
100011242
3.

BL21_37_4_1

Organism:
Escherichia coli
Source name:
cell culture
Platform:
GPL11242
Series:
GSE25561
Download data: TXT
Sample
Accession:
GSM628239
ID:
300628239
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