Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions.
暂无分享,去创建一个
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.
[1] J. Dixon,et al. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. , 1991, Analytical biochemistry.
[2] J. McCafferty,et al. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression , 2004, BMC biotechnology.
[3] F. McCormick,et al. Signal transduction from multiple Ras effectors. , 1997, Current opinion in genetics & development.