GSTA2
GSTA2 (glutathione S-transferase alpha 2, also known as GST2) is a cytoplasmic alpha-class glutathione S-transferase. It catalyses the conjugation of glutathione to a wide range of electrophilic compounds, supporting cellular detoxification. Browse Assay Genie's current range of GSTA2 research reagents below, or read on for the biology behind the target.
GSTA2 catalyses the conjugation of glutathione to a large variety of electrophilic compounds. This activity underlies the role of glutathione S-transferases in detoxifying carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. Like other alpha-class enzymes, GSTA2 also shows glutathione peroxidase activity, which helps protect cells from reactive oxygen species and the products of peroxidation. Alpha-class enzymes are also described as metabolising bilirubin and certain anti-cancer drugs in the liver.
The GSTA2 gene encodes a member of the alpha class, which belongs to the GST superfamily. Mammalian soluble cytoplasmic glutathione S-transferases fall into eight classes: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The alpha-class genes sit together in a cluster on chromosome 6, and these enzymes are the most abundantly expressed glutathione S-transferases in liver. The protein localises to the cytoplasm. Orthologues are annotated in mouse and rat, both named Gsta2.
Glutathione S-transferase genes are known to be highly polymorphic. These variants can change an individual's susceptibility to carcinogens and toxins, and can affect the toxicity and efficacy of some drugs, which is why the family is widely studied in toxicology and pharmacogenetics. HGNC lists GSTA2 in the soluble glutathione S-transferases gene group, with GST2 as an alias and glutathione S-transferase A2 as a previous name.
GSTA2 conjugates glutathione to electrophilic compounds, including carcinogens, drugs and environmental toxins, making it a focus for studies of cellular detoxification.
Alpha-class enzymes show glutathione peroxidase activity, protecting cells from reactive oxygen species and the products of peroxidation.
Alpha-class glutathione S-transferases are the most abundantly expressed GSTs in liver, where they metabolise bilirubin and certain anti-cancer drugs.
Polymorphisms in GST genes can alter susceptibility to carcinogens and toxins and affect drug toxicity and efficacy, so GSTA2 is relevant to variability studies.
GSTA2 catalyses the conjugation of glutathione to a large variety of electrophilic compounds. This detoxifies carcinogens, drugs, environmental toxins and products of oxidative stress. As an alpha-class enzyme it also has glutathione peroxidase activity, protecting cells from reactive oxygen species and peroxidation products.
The HGNC-approved name is glutathione S-transferase alpha 2. UniProt uses glutathione S-transferase A2, and GST2 is a recorded alias. The enzyme carries the EC number 2.5.1.18 and sits in the soluble glutathione S-transferases gene group.
Mouse and rat each have an orthologue named Gsta2. In humans, glutathione S-transferase genes are highly polymorphic, and such variation can change susceptibility to carcinogens and toxins and influence drug toxicity and efficacy. Check the datasheet of any product for its validated reactivity.
Other alpha-class glutathione S-transferases from the same gene cluster, relevant to detoxification and oxidative stress research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09210; product specifications from Assay Genie datasheets.