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Immunoaffinity Purification of Protein Complexes from Mammalian Cells

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Gene Regulation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 977))

Abstract

In this chapter, we describe a purification scheme designed to isolate multisubunit protein complexes gently and quickly from crude extracts of mammalian cells using immunoaffinity purification of epitope tagged proteins and the multisubunit complexes with which they associate. As an example we describe isolation of the mammalian Mediator complex from HeLa S3 cells.

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Acknowledgments

Work in the authors’ laboratory is supported by grant GM41628 from the National Institute of General Medicine, a grant to the Stowers Institute for Medical Research from the Helen Nelson Medical Research Fund at the Greater Kansas City Community Foundation, and the Stowers Institute for Medical Research.

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Tomomori-Sato, C., Sato, S., Conaway, R.C., Conaway, J.W. (2013). Immunoaffinity Purification of Protein Complexes from Mammalian Cells. In: Bina, M. (eds) Gene Regulation. Methods in Molecular Biology, vol 977. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-284-1_22

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  • DOI: https://doi.org/10.1007/978-1-62703-284-1_22

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-283-4

  • Online ISBN: 978-1-62703-284-1

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