GSTM1 Rabbit Polyclonal Antibody

GSTM1 is an important member of the Mu class within the cytosolic glutathione S-transferase (GST) superfamily, primarily encoded by the GSTM1 gene. The protein functions as a dimeric enzyme, with its active site containing a conserved serine residue that catalyzes the conjugation of reduced glutathione (GSH) with a variety of electrophilic xenobiotics—such as environmental carcinogens, drugs, and oxidative stress products—generating more water-soluble mercapturic acid derivatives, thereby facilitating the detoxification and excretion of these potentially toxic compounds. In addition to its classical detoxification function, GSTM1 also participates in regulating cellular redox balance, protecting cells from reactive oxygen species (ROS)-induced damage through both direct and indirect mechanisms. In human populations, the GSTM1 gene exhibits extensive polymorphism, with the most common being a homozygous deletion variant (GSTM1-null), which results in a complete loss of enzyme activity in affected individuals. Epidemiological studies have shown that the GSTM1-null genotype is strongly associated with increased susceptibility to various cancers, including lung, bladder, and gastric cancers, as individuals carrying this genotype have significantly impaired capacity to detoxify environmental carcinogens. Furthermore, GSTM1 expression and activity also influence the metabolic efficiency of numerous drugs and individual susceptibility to oxidative stress-related diseases such as chronic obstructive pulmonary disease and cardiovascular disease, making it an important biomarker in pharmacogenomics and personalized medicine.