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• W1570346075 abstract "pGEX vectors and glutathione S-transferase (GST) are useful for expressing polypeptides in heterologous systems. This chapter discusses the role of GST as an affinity tag for fusion proteins. The methods described in the chapter refer to GST fusions expressed in E. coli and may require adaptation for eukaryotic systems. The major reason for using GST as a fusion partner is that many fusions remain soluble and stable even at high levels of expression and can be purified by affinity chromatography under nondenaturing conditions. GST fusion is used as antigens for immunological or vaccination studies or as a way of producing functionally active enzymes for biochemical or structural studies. A particularly fruitful application has been the use of GST fusion proteins in the analysis of protein–DNA and protein–protein interactions. Typically, a GST fusion protein acts as bait to purify specifically interacting proteins that are then isolated by affinity purification with glutathione–agarose beads. A related application has been to use the pGEX plasmids to construct a complementary DNA (cDNA) expression library, which was then probed with DNA or protein probes to identify novel DNA-binding or protein-binding domains. Larger cDNA expression libraries can be constructed using the bacteriophage expression vector λGEX5J. Another important advancement has been the development of a variety of eukaryotic versions of the pGEX vectors that allow proteins to be produced outside of the reducing environment of the bacterial cell so that proteins can fold in a more native fashion and permit posttranslational modifications—such as glycosylation and phosphorylation." @default.
• W1570346075 created "2016-06-24" @default.
• W1570346075 creator A5082252071 @default.
• W1570346075 date "2000-01-01" @default.
• W1570346075 modified "2023-09-27" @default.
• W1570346075 title "[17] Generating fusions to glutathione S-transferase for protein studies" @default.
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• W1570346075 doi "https://doi.org/10.1016/s0076-6879(00)26059-x" @default.
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