title: Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions.
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.
authors: Department of Pharmacology & Toxicology, MCW Cancer Center, Medical College of Wisconsin, Milwaukee, WI, 53202, USA, hvikis@gmail.com.
authors: Haris G
authors: HG
authors: Vikis
authors: Kun-Liang
authors: KL
authors: Guan
mesh_terms: D000906:Antibodies / Q000737:chemistry / Q000276:immunology; D001665:Binding Sites; D002846:Chromatography, Affinity; D005982:Glutathione Transferase / Q000737:chemistry / Q000276:immunology; D027384:Oncogene Proteins v-raf / Q000737:chemistry*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D060066:Protein Interaction Maps; D018631:ras Proteins / Q000737:chemistry*
chemical_list: D000906:Antibodies; D005982:Glutathione Transferase; D027384:Oncogene Proteins v-raf; D018631:ras Proteins