For the measurement of total GST activity (cytosolic and microsomal)
Features
  • Measure GST activity in plasma, tissue homogenates, and cell lysates
  • Assay 22 samples in duplicate
  • Measure GST activity down to 24 U/ml
  • Plate-based colorimetric measurement (340 nm)
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Glutathione S-Transferase Assay Kit

Item No. 703302

Technical Information
Synonyms
  • GST Assay Kit
Origin
Animal/Horse
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes, which play a key role in cellular detoxification. The enzymes protect cells against toxicants by conjugating them to glutathione, thereby neutralizing their electrophilic sites, and rendering the products more water-soluble.1 The glutathione conjugates are metabolized further to mercapturic acid and then excreted.1 Based on their sequence homology, substrate specificity, and immunological cross-reactivity, GSTs have been grouped into species-independent classes of isozymes.2,3,4,5 These classes are comprised of cytosolic enzymes and the fifth form is microsomal.2,3,4,5 The Cayman Chemical Glutathione S-Transferase Assay Kit measures total GST activity (cytosolic and microsomal) by measuring the conjugation of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione.6 The conjugation is accompanied by an increase in absorbance at 340 nm. The rate of increase is directly proportional to the GST activity in the sample. The Cayman GST Assay Kit can be used to measure GST activity in plasma, erythrocyte lysates, tissue homogenates, and cell lysates. Cytosolic and microsomal GST activity can also be assayed separately.

    Needed but not supplied: Please download the kit booklet to verify if UltraPure Water (Milli-Q or equivalent) or any other components are needed for this assay.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Boyland, E., and Chasseaud, L.F. The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis. Adv. Enzymol. Relat. Areas Mol. Biol. 32, 173-219 (1969).

    2. Mannervik, B. The isoenzymes of glutathione transferase. Adv. Enzymol. Relat. Areas Mol. Biol. 57, 357-417 (1985).

    3. Mannervik, B., Ålin, P., Guthenberg, C., et alIdentification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. USA 82, 7202-7206 (1985).

    4. Morgenstern, R., DePierre, J.W., and Ernster, L. Activation of microsomal glutathione S-transferase activity by sulfhydryl reagents. Biochem. Biophys. Res. Commun. 87, 657-663 (1979).

    5. Jakoby, W.B. The glutathione S-transferases: A group of multifunctional detoxification proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 46, 383-414 (1978).

    6. Habig, W.H., Pabst, M.J., and Jakoby, W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. The Journal of Biological Chemisty 249, 7130-7139 (1974).

    Product Citations

    Moehlman, A.T., Kanfer, G., and youle, R.J. Loss of STING in parkin mutant flies suppresses muscle defects and mitochondria damage. PLos Genet. 19(7), e1010828 (2023).

    Kowalska, K., and Milnerowicz, H. The influence of age and gender on the pro/antioxidant status in young healthy people. Ann. Clin. Lab. Sci. 46(5), 480-488 (2016).