| Literature DB >> 15064458 |
Haris G Vikis1, Kun-Liang Guan.
Abstract
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.Entities:
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Year: 2004 PMID: 15064458 DOI: 10.1385/1-59259-762-9:175
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745