A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF

A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF

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 misf...

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Main Authors: Thomson, Christy A., Olson, Melanie, Jackson, Linda M., Schrader, John W.
Format: Online
Language:English
Published: Public Library of Science 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498172/
id pubmed-3498172
recordtype oai_dc
spelling pubmed-34981722012-11-19 A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF Thomson, Christy A. Olson, Melanie Jackson, Linda M. Schrader, John W. Research Article 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. Public Library of Science 2012-11-14 /pmc/articles/PMC3498172/ /pubmed/23166789 http://dx.doi.org/10.1371/journal.pone.0049891 Text en © 2012 Thomson et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Thomson, Christy A.
Olson, Melanie
Jackson, Linda M.
Schrader, John W.
spellingShingle Thomson, Christy A.
Olson, Melanie
Jackson, Linda M.
Schrader, John W.
A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
author_facet Thomson, Christy A.
Olson, Melanie
Jackson, Linda M.
Schrader, John W.
author_sort Thomson, Christy A.
title A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
title_short A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
title_full A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
title_fullStr A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
title_full_unstemmed A Simplified Method for the Efficient Refolding and Purification of Recombinant Human GM-CSF
title_sort simplified method for the efficient refolding and purification of recombinant human gm-csf
description 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.
publisher Public Library of Science
publishDate 2012
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498172/
_version_ 1611924148614856704

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