Glutathione-S-transferase-fusion based assays for studying protein-protein interactions. Methods Mol Biol 2004;261:175-86
Date
04/06/2004Pubmed ID
15064458DOI
10.1385/1-59259-762-9:175Scopus ID
2-s2.0-3242675407 (requires institutional sign-in at Scopus site) 65 CitationsAbstract
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.
Author List
Vikis HG, Guan KLMESH terms used to index this publication - Major topics in bold
AnimalsChromatography, Affinity
Glutathione Transferase
Humans
Protein Binding
Protein Interaction Mapping
Recombinant Fusion Proteins
