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Updated: Apr 15, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
Published on: July 21, 2021
Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions
Haris G Vikis1, Kun-Liang Guan
1Department of Pharmacology & Toxicology, MCW Cancer Center, Medical College of Wisconsin, Milwaukee, WI, 53202, USA, hvikis@gmail.com.
Abstract:
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.

