The solution contains 1mg/ml of the antibody in a buffer consisting of PBS at pH 7.4 and 0.1% Sodium Azide.
Glutathione-S-Transferases (GSTs) are a diverse family of enzymes that play a crucial role in cellular detoxification processes. These enzymes catalyze the conjugation of the tripeptide glutathione (GSH) to a variety of endogenous and exogenous electrophilic compounds. This reaction is essential for the detoxification of harmful substances, including carcinogens, environmental toxins, and products of oxidative stress .
GSTs are found in virtually all eukaryotic and prokaryotic organisms. They are classified into several classes based on their sequence homology and substrate specificity, including Alpha, Mu, Pi, Theta, and Omega classes . Each class has distinct structural features and catalytic properties:
GSTs have a conserved structure with two distinct domains: a smaller N-terminal domain that binds GSH and a larger C-terminal domain that binds the electrophilic substrate. The active site of GSTs contains a serine or cysteine residue that plays a critical role in the catalytic mechanism .
GSTs have been extensively studied for their applications in biotechnology and medicine. They are used as fusion tags in protein expression systems to facilitate the purification of recombinant proteins. The GST tag allows for easy purification using glutathione-affinity chromatography .
In medicine, GSTs are explored as potential biomarkers for various diseases, including cancer. The overexpression of GST Pi (GSTP1) in tumors is associated with resistance to chemotherapy, making it a target for cancer therapy .
Antibodies against GST are valuable tools in research and diagnostics. These antibodies can be used to detect and quantify GST-tagged proteins in various applications, including Western blotting, immunoprecipitation, and immunofluorescence . GST antibodies are typically generated by immunizing animals with purified GST protein or GST fusion proteins. The resulting polyclonal or monoclonal antibodies are then purified and characterized for their specificity and affinity .