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BioReagent BioReagent for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Glutathione S-transferase (GST) is a protein family with diverse physiological functions, primarily located within the cytoplasm. GST serves as a crucial component of the body's detoxification enzyme system. It mainly catalyzes the covalent conjugation of various chemicals and their metabolites with the sulfhydryl group of glutathione (GSH), transforming electrophilic compounds into hydrophilic metabolites. These conjugated products are then readily excreted via bile or urine, thereby achieving the detoxification and elimination of various potentially or overtly toxic substances from the body. Consequently, GST plays a vital biological role in protecting cells from damage caused by electrophilic compounds. Furthermore, because GST exhibits glutathione peroxidase (GSH-Px) activity, it is also referred to as non-selenium-dependent GSH-Px (non-Se GSH-Px) and functions in repairing oxidatively damaged macromolecules such as DNA and proteins. Note: The reaction catalyzed by GST decreases GSH levels but does not increase oxidized glutathione (GSSG) content. Assay Principle: GST catalyzes the conjugation of GSH with 1-chloro-2,4-dinitrobenzene (CDNB). The resulting conjugate has a maximum absorption peak at a wavelength of 340 nm. By measuring the rate of increase in absorbance at 340 nm, the activity of GST can be calculated.
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