Title | GST Pull-down. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Einarson MB, Pugacheva EN, Orlinick JR |
Journal | CSH Protoc |
Volume | 2007 |
Pagination | pdb.prot4757 |
Date Published | 2007 Aug 01 |
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. One of these applications is their use as probes for the identification of protein-protein interactions. The pull-down method described in this protocol is fundamentally similar to immunoprecipitation. Immunoprecipitation is based on the ability of an antibody to bind to its antigen in solution, and the subsequent purification of the immunocomplex by collection on protein A- or G-coupled beads. Similarly, the GST pull-down is an affinity capture of one or more proteins (either defined or unknown) in solution by its interaction with the GST fusion probe protein and subsequent isolation of the complex by collection of the interacting proteins through the binding of GST to glutathione-coupled beads. |
DOI | 10.1101/pdb.prot4757 |
Alternate Journal | CSH Protoc |
PubMed ID | 21357137 |
Submitted by kej2006 on June 6, 2018 - 4:10pm