GSTP1
GSTP1 (glutathione S-transferase pi 1, also known as GSTP, GST3 and FAEES3) is a soluble glutathione S-transferase that conjugates reduced glutathione to hydrophobic electrophiles. It contributes to xenobiotic detoxification and to the regulation of ferroptosis. Browse Assay Genie's current range of GSTP1 research reagents below, or read on for the biology behind the target.
GSTP1 catalyses the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. This is the central step in the detoxification role of glutathione S-transferases. The enzyme is involved in forming glutathione conjugates of prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2), and it participates in the formation of novel hepoxilin regioisomers.
The protein also acts as a negative regulator of ferroptosis. It does so by mediating glutathione conjugation and detoxification of the reactive aldehyde 4-hydroxynonenal (4-HNE). In addition, GSTP1 negatively regulates CDK5 activity through p25/p35 translocation, a function that helps prevent neurodegeneration. UniProt records the protein in the cytoplasm, mitochondrion and nucleus.
The GSTP1 gene encodes a member of the GST superfamily, pi family. Soluble GSTs are grouped into four main classes (alpha, mu, pi and theta) on the basis of their biochemical, immunologic and structural properties. HGNC places the gene in the soluble glutathione S-transferases group. According to the NCBI Gene summary, GSTP1 is polymorphic and encodes active but functionally different variant proteins. These variants are thought to act in xenobiotic metabolism and to play a role in susceptibility to cancer and other diseases. Mouse and rat both carry a Gstp1 ortholog, which supports comparative studies in rodent models.
GSTP1 conjugates glutathione to hydrophobic electrophiles, making it a key enzyme for studying detoxification of foreign and endogenous compounds.
GSTP1 negatively regulates ferroptosis by conjugating glutathione to 4-hydroxynonenal, linking it to lipid peroxidation-derived aldehyde detoxification.
The polymorphic GSTP1 gene encodes functionally different variants thought to influence susceptibility to cancer and other diseases.
GSTP1 negatively regulates CDK5 activity via p25/p35 translocation, which is relevant to work on preventing neurodegeneration.
GSTP1 catalyses the conjugation of reduced glutathione to many hydrophobic electrophiles, including prostaglandin A2 and J2. It also detoxifies 4-hydroxynonenal to restrain ferroptosis, and it negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
The official name is glutathione S-transferase pi 1. Aliases include GSTP, GST3 and FAEES3, and UniProt lists the protein as Glutathione S-transferase P. The enzyme is classified as EC 2.5.1.18 and belongs to the pi family of the GST superfamily.
NCBI describes GSTP1 as polymorphic, with functionally different variant proteins thought to affect susceptibility to cancer and other diseases. Mouse and rat each have a Gstp1 ortholog; check the datasheet of any product for its validated reactivity.
Other glutathione S-transferases, ferroptosis regulators and CDK5 pathway proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09211; product specifications from Assay Genie datasheets.