Glutathione-S-Transferase (GST) is a family of enzymes involved in the detoxification process by catalyzing the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates. This process is crucial for the detoxification of endogenous compounds such as peroxidized lipids and the breakdown of xenobiotics . GSTs are found in both eukaryotic and prokaryotic organisms and are known for their role in phase II metabolism .
GSTs are dimeric enzymes that can constitute up to 10% of cytosolic protein in some mammalian organs . They catalyze the conjugation of GSH via a sulfhydryl group to electrophilic centers on a wide variety of substrates, making the compounds more water-soluble and facilitating their excretion from the body . The GST family consists of three superfamilies: cytosolic, mitochondrial, and microsomal (also known as MAPEG) proteins .
The mouse antibody peroxidase conjugated to GST is a specialized tool used in various immunoassays. Horseradish peroxidase (HRP) is a 44 kDa glycoprotein commonly conjugated to antibodies for use in applications such as ELISA, immunohistochemistry, and western blotting . The enzyme label can be visualized through chromogenic reactions, making it a valuable tool for detecting and quantifying target proteins .