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. 2013:977:273-87.
doi: 10.1007/978-1-62703-284-1_22.

Immunoaffinity purification of protein complexes from Mammalian cells

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Immunoaffinity purification of protein complexes from Mammalian cells

Chieri Tomomori-Sato et al. Methods Mol Biol. 2013.

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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Figures

Figure 1
Figure 1
Scheme For Immunoaffinity Purification of Protein Complexes
Figure 2
Figure 2
Immunoaffinity Purified Mammalian Mediator Complex From HeLa S3 Nuclear Extract Through FLAG-tagged Mediator Subunits.
Figure 3
Figure 3
Micro Bio-Spin Chromatography Column Used to Remove Residual Beads From Immunoaffinity Purified Fractions

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