Glutathione-S-transferase (GST)-fusion proteins have become an effective reagent to use in the study of protein-protein interactions. GST-fusion proteins can be produced in bacterial and mammalian cells in large quantities and purified rapidly. GST can be coupled to a glutathione matrix, which permits its use as an effective affinity column to study interactions in vitro or to purify protein complexes in cells expressing the GST-fusion protein. Here, we provide a technical description of the utilization of GST-fusion proteins as both a tool to study protein-protein interactions and also as a means to purify interacting proteins.
CITATION STYLE
Vikis, H. G., & Guan, K. L. (2015). Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions. Methods in Molecular Biology, 1278, 353–364. https://doi.org/10.1007/978-1-4939-2425-7_22
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