title: Identification of Protein-Protein Interactions with Glutathione-S-Transferase (GST) Fusion Proteins.
abstract: INTRODUCTIONGlutathione-S-transferase (GST) fusion proteins have had a wide range of applications since their introduction as tools for synthesis of recombinant proteins in bacteria. GST was originally selected as a fusion moiety because of several desirable properties. First and foremost, when expressed in bacteria alone, or as a fusion, GST is not sequestered in inclusion bodies (in contrast to previous fusion protein systems). Second, GST can be affinity-purified without denaturation because it binds to immobilized glutathione, which provides the basis for simple purification. Consequently, GST fusion proteins are routinely used for antibody generation and purification, protein-protein interaction studies, and biochemical analysis. This article describes the use of GST fusion proteins as probes for the identification of protein-protein interactions.
authors.forename: Margret B
authors.initials: MB
authors.lastname: Einarson
authors.forename: Elena N
authors.initials: EN
authors.lastname: Pugacheva
authors.forename: Jason R
authors.initials: JR
authors.lastname: Orlinick