Abstract
Glutathione-S-transferase (GST)-fusion proteins have become an effective reagent to use in the study of protein-protein interactions. They can be produced in bacterial and mamMalian cells in large quantities and purified rapidly. Given that GST can be coupled to a glutathione matrix permits its use as an effective affinity column to study interactions in vitro or to purify protein complexes in cells expressing the GST-fusion. Here we provide a technical description on the utilization of GST-fusion proteins as both a tool to studying protein-protein interactions and also as a means to purify interacting proteins.
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References
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© 2004 Humana Press Inc., Totowa, NJ
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Vikis, H.G., Guan, KL. (2004). Glutathione-S-Transferase-Fusion Based Assays for Studying Protein-Protein Interactions. In: Fu, H. (eds) Protein-Protein Interactions. Methods in Molecular Biology, vol 261. Humana Press. https://doi.org/10.1385/1-59259-762-9:175
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DOI: https://doi.org/10.1385/1-59259-762-9:175
Publisher Name: Humana Press
Print ISBN: 978-1-58829-120-2
Online ISBN: 978-1-59259-762-8
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