Glutathione-S-Transferase (GST) is a crucial enzyme involved in the detoxification processes within cells. It catalyzes the conjugation of the reduced form of glutathione (GSH) to various electrophilic compounds, facilitating their excretion from the body. GSTs are found in both eukaryotic and prokaryotic organisms and play a significant role in protecting cells from oxidative stress and toxic substances.
GSTs are a family of enzymes that typically exist as homodimers or heterodimers. Each subunit has a molecular weight of approximately 26 kDa . The enzyme’s active site binds to GSH and the substrate, promoting the nucleophilic attack of GSH on the substrate, resulting in the formation of a glutathione conjugate.
In molecular biology and biochemistry, GST is often used as a fusion tag to facilitate the purification and detection of recombinant proteins. The GST tag is fused to the protein of interest, and the fusion protein can be purified using glutathione-affinity chromatography. This method leverages the high affinity of GST for glutathione, allowing for efficient purification of the tagged protein.
Mouse monoclonal antibodies against GST are widely used in research to detect and quantify GST-tagged proteins. These antibodies are produced by immunizing mice with a purified recombinant GST fusion protein, leading to the generation of hybridoma cells that secrete the desired antibody .
Mouse monoclonal antibodies against GST are invaluable tools in research. They are used to: