Anti-GSTM2 / Glutathione S-transferase Mu 2

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. GSTM2 antibody detects Glutathione S-transferase Mu 2, an enzyme involved in detoxification and cellular defense against oxidative stress. The UniProt recommended name is Glutathione S-transferase Mu 2 (GSTM2). This cytosolic enzyme catalyzes the conjugation of reduced glutathione to a wide variety of electrophilic compounds, promoting their solubility and excretion while protecting macromolecules from oxidative and chemical damage.Functionally, GSTM2 antibody identifies a 218-amino-acid enzyme belonging to the Mu class of the glutathione S-transferase family. GSTM2 participates in phase II detoxification pathways by binding and neutralizing toxic metabolites, drugs, and environmental carcinogens. It exhibits substrate specificity toward lipid peroxidation products, reactive oxygen species intermediates, and xenobiotic compounds. GSTM2 is also involved in modulating signaling pathways such as JNK and MAPK, linking oxidative stress defense to cell survival and apoptosis regulation.The GSTM2 gene is located on chromosome 1p13.3 and is primarily expressed in liver, skeletal muscle, and brain. Its expression levels vary between individuals due to polymorphisms in the GSTM gene cluster, influencing susceptibility to toxins and disease. As a member of the Mu family, GSTM2 functions alongside other isoenzymes (GSTM1-GSTM5) to maintain redox balance and detoxification capacity.Pathologically, reduced GSTM2 expression or polymorphic variants have been associated with increased risk of cancer, neurodegenerative disease, and drug-induced toxicity. Elevated GSTM2 levels can enhance cellular resistance to chemotherapy and oxidative damage. Research using GSTM2 antibody supports studies in toxicology, pharmacogenomics, and oxidative stress biology.GSTM2 antibody is validated for western blotting, immunohistochemistry, and ELISA to detect detoxification enzymes. NSJ Bioreagents provides GSTM2 antibody reagents optimized for research in redox regulation, xenobiotic metabolism, and antioxidant defense.Structurally, Glutathione S-transferase Mu 2 forms a homodimer with each subunit containing a glutathione-binding (G-site) domain and a hydrophobic substrate-binding (H-site). Its tertiary structure supports efficient conjugation reactions and dynamic interaction with glutathione substrates. This antibody enables investigation of GSTM2's function in metabolic detoxification and cellular stress response.