Glutathione-S-transferases (GSTs) are dimeric proteins, which belongs to phase II detoxification enzymes family. The highly polymorphic human cytosolic GSTs are divided into six classes, such as, α, μ, ω, π, θ, and ζ.
The antibody is specific for native as well as denatured-reduced forms of glutathione-S-transferase from Schistosoma japonicum. Anti-GST may be used in various immunoassays to identify the expression of GST fusion proteins.
Immunogen
recombinant GST from Schistosoma japonicum expressed in E. coli.
Application
Immunoprecipitation was performed on NIH 3T3 cells transiently transfected with GST fusion proteins. IP was performed using agarose-linked rabbit anti-GST IgG with mixing for 2 hours at 4 degrees.
Rabbit Anti-Glutathione-S-Transferase (GST)-Agarose antibody can be used for ELISA, immunoaffinity purification and immunoprecipitation assays.
Biochem/physiol Actions
Glutathione-S-transferases (GSTs) can catalyse the conjugation of glutathione (GSH) to various endogenous and exogenous electrophilic compounds. The π and μ classes of GSTs controls the mitogen-activated protein (MAP) kinase pathway. It can also serve as transport proteins.
Physical form
Suspension in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
Preparation Note
Prepared by coupling cyanogen bromide-activated agarose at 7-8 mg antibody per mL resin volume.
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The Journal of biological chemistry, 282(12), 8801-8811 (2007-02-03)
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