GSTM1
GSTM1 (glutathione S-transferase mu 1) is a cytoplasmic mu-class glutathione S-transferase that conjugates reduced glutathione to hydrophobic electrophiles. It is also known as MU, H-B and GST1, and was previously named glutathione S-transferase M1. Browse Assay Genie's current range of GSTM1 research reagents below, or read on for the biology behind the target.
GSTM1 catalyses the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTM1 is also involved in forming glutathione conjugates of prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2), and participates in the formation of novel hepoxilin regioisomers.
The GSTM1 protein belongs to the GST superfamily and the mu family. It is a soluble, cytoplasmic enzyme and is classed by HGNC in the soluble glutathione S-transferases gene group. Cytosolic and membrane-bound glutathione S-transferases are encoded by two distinct supergene families. Eight classes of soluble cytoplasmic mammalian enzyme have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mouse and rat orthologs are both named Gstm1.
The GSTM1 gene sits in a cluster of mu-class genes on chromosome 1p13.3, and these genes are known to be highly polymorphic. Such variation can change an individual's susceptibility to carcinogens and toxins, and can affect the toxicity and efficacy of certain drugs. Null mutations of this mu-class gene have been linked with an increase in a number of cancers, likely because of increased susceptibility to environmental toxins and carcinogens. Transcript variants of the gene encode multiple protein isoforms.
GSTM1 conjugates glutathione to electrophiles such as carcinogens, therapeutic drugs and environmental toxins, making it a focus for studies of detoxification.
The mu class acts on products of oxidative stress, so GSTM1 is relevant to research on how cells handle reactive electrophilic damage.
Null mutations of this mu-class gene have been linked with increased numbers of cancers, supporting its use in studies of carcinogen susceptibility.
Polymorphic variation in the mu-class gene cluster can affect drug toxicity and efficacy, which makes GSTM1 relevant to pharmacogenetic research.
GSTM1 catalyses the conjugation of reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. This supports detoxification of carcinogens, drugs, environmental toxins and oxidative stress products. It also forms glutathione conjugates of PGA2 and PGJ2 and takes part in forming novel hepoxilin regioisomers.
GSTM1 is also known as MU, H-B and GST1, and was previously called glutathione S-transferase M1. The UniProt protein name is Glutathione S-transferase Mu 1. Transcript variants of the GSTM1 gene encode multiple protein isoforms, so check the datasheet of any product for its validated reactivity.
The GSTM1 gene is highly polymorphic, and variants can change susceptibility to carcinogens and toxins and alter drug toxicity and efficacy. Null mutations of this mu-class gene have been linked with an increase in a number of cancers, likely through greater susceptibility to environmental toxins and carcinogens.
Other mu-class glutathione S-transferases from the same gene cluster, with related products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09488; product specifications from Assay Genie datasheets.