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Glutathione S-transferase 3 (GST3), also known as GST-Pi, is an enzyme that catalyzes the conjugation of glutathione (GSH) to the electrophilic center of various phase I toxic xenobiotic metabolites, facilitating their excretion by phase III membrane channels, transporters, and pumps.1 It functions as a homodimer, with each monomer containing an N-terminal GSH-binding domain and a C-terminal domain with a hydrophobic cavity (H-site) for toxic compound binding. GST3 is expressed primarily in erythrocytes, as well as in the brain, heart, lung, testis, skin, kidney, pancreas, and saliva. GST3 dimers can bind a nitric oxide (NO) carrier, such as S-nitrosoglutathione or dinitrosyl-diglutathionyl-iron complex (DNDGIC), with one active site, indicating a role in the storage and transport of NO, while maintaining detoxification activity in the second active site.2 Expression of GSTP1, the gene encoding GST3, is increased in patients with advanced-stage chronic kidney disease. GSTP1 polymorphisms are associated with increased risk of Parkinson's disease following exposure to cigarette smoke or pesticides, as well as with amyotrophic lateral sclerosis. Cayman's GST3/GST-Pi (C-Term) Rabbit Monoclonal Antibody (Clone RM347) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Glutathione Transferase P1-
2. Human glutathione transferase P1-