Glutathione-S-transferase (GST) fusion proteins are used in a wide variety of applications in the lab. GST was originally selected as a fusion moiety because it’s not sequestered in inclusion bodies when expressed in bacteria and it can be affinity-purified without denaturation. Purification is fairly straightforward process, and GST fusion proteins are routinely used for antibody generation and purification, protein-protein interaction studies, and biochemical analysis.

Protocols describing the use of GST fusion proteins are among our most popular, and November’s issue of Cold Spring Harbor Protocols brings two new sets of instructions, covering Preparation of Soluble GST Fusion Proteins and Preparation of Insoluble GST Fusion Proteins. These articles complement our already extensive coverage, which includes the previously featured (and still freely available) article Preparation of GST Fusion Proteins. Our readers also frequently access Identification of Protein-Protein Interactions with Glutathione-S-Transferase (GST) Fusion Proteins, GST Pull-down, Detection of Protein-Protein Interactions Using the GST Fusion Protein Pulldown Technique, Detection of Protein-Protein Interactions Using Far Western with GST Fusion Proteins, Far Western: Labeling GST Fusion Proteins, and Far Western: Probing Membranes.