Gateway vectors for the production of combinatorially‐tagged His6‐MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli

@article{Nallamsetty2005GatewayVF,
  title={Gateway vectors for the production of combinatorially‐tagged His6‐MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli},
  author={Sreedevi Nallamsetty and B. P. Austin and K. Penrose and D. Waugh},
  journal={Protein Science},
  year={2005},
  volume={14}
}
  • Sreedevi Nallamsetty, B. P. Austin, +1 author D. Waugh
  • Published 2005
  • Medicine, Chemistry
  • Protein Science
  • Many proteins that accumulate in the form of insoluble aggregates when they are overproduced in Escherichia coli can be rendered soluble by fusing them to E. coli maltose binding protein (MBP), and this will often enable them to fold in to their biologically active conformations. Yet, although it is an excellent solubility enhancer, MBP is not a particularly good affinity tag for protein purification. To compensate for this shortcoming, we have engineered and successfully tested Gateway… CONTINUE READING

    Topics from this paper.

    Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli
    • 15
    • Open Access
    A dual protease approach for expression and affinity purification of recombinant proteins
    • 8
    • Open Access

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 33 REFERENCES
    Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
    • 58
    • Open Access
    Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies.
    • 159
    • Open Access
    Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • 909
    • Open Access
    Expression and purification of recombinant proteins by fusion to maltose-binding protein
    • 102
    • Highly Influential
    Maltodextrin‐binding proteins from diverse bacteria and archaea are potent solubility enhancers
    • 112
    • Open Access