Expression, refolding and purification of a human interleukin-17A variant.

@article{Wu2011ExpressionRA,
  title={Expression, refolding and purification of a human interleukin-17A variant.},
  author={Bingyuan Wu and Jennifer F. Nemeth and Dariusz J. Janecki and Brian Jones and Galina Obmolova and Thomas J. Malia and Audrey Baker and Deidra Bethea and M Merle Elloso and Michael Naso and Susann Taudte},
  journal={Cytokine},
  year={2011},
  volume={53 1},
  pages={
          107-14
        }
}
A human interleukin-17A (IL-17A) variant was overexpressed in Escherichia coli BL21 (DE3) under the control of a T(7) promoter. The resulting insoluble inclusion bodies were isolated and solubilized by homogenization with 6 M guanidine HCl. The denatured recombinant human IL-17A variant was refolded in 20 mM Tris-HCl, pH 9.0, 500 mM arginine, 500 mM guanidine HCl, 15% glycerol, 1 mM cystamine, and 5 mM cysteine at 2-8°C for 40 h. The refolded IL-17A variant was subsequently purified using a… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 15 REFERENCES

Identification of an interleukin 17F/17A heterodimer in activated human CD4+ T cells

JF Wright, YJ Guo, +3 authors YC Qiu
  • J Biol Chem 2007;282:13447–55
  • 2007
VIEW 1 EXCERPT

IL-17 cytokine family.

  • The Journal of allergy and clinical immunology
  • 2004
VIEW 1 EXCERPT

Protein refolding for industrial processes.

  • Current opinion in biotechnology
  • 2001
VIEW 1 EXCERPT