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Biophysics - Hematology - Immunology - Rheumatology


A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
Published: Wednesday, November 14, 2012
Author: Christy A. Thomson et al.

by Christy A. Thomson, Melanie Olson, Linda M. Jackson, John W. Schrader

Human granulocyte macrophage colony-stimulating factor (hGM-CSF) is a haematopoietic growth factor and proinflammatory cytokine. Recombinant hGM-CSF is important not only as a research tool but also as a biotherapeutic. However, rhGM-CSF expressed in E. coli is known to form inclusion bodies of misfolded, aggregated protein. Refolding and subsequent purification of rhGM-CSF from inclusion bodies is difficult with low yields of bioactive protein being produced. Here we describe a method for the isolation, refolding and purification of bioactive rhGM-CSF from inclusion bodies. The method is straightforward, not requiring extensive experience in protein refolding nor purification and using standard laboratory equipment.
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