Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates.

@article{Haacke2009ChaperoneOI,
  title={Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates.},
  author={Annette Haacke and Gabriele Fendrich and Paul Ramage and Martin Geiser},
  journal={Protein expression and purification},
  year={2009},
  volume={64 2},
  pages={185-93}
}
The recombinant expression of eukaryotic proteins in Escherichia coli often results in protein aggregation. Several articles report on improved solubility and increased purification yields of individual proteins upon over-expression of E. coli chaperones but this effect might potentially be protein-specific. To find out whether chaperone over-expression is a generally applicable strategy for the production of human protein kinases in E. coli, we analyzed 10 kinases, mainly as catalytic domain… CONTINUE READING
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