GPX1 Human

GPx1 is the most abundant version of glutathione peroxidase, found in the cytoplasm of nearly all mammalian tissues . The enzyme’s primary function is to detoxify hydrogen peroxide (H₂O₂) by reducing it to water (H₂O), using glutathione (GSH) as a substrate. This reaction is crucial for maintaining cellular redox balance and protecting cells from oxidative stress .

Recombinant Human Glutathione Peroxidase 1 is a human full-length protein, typically expressed in Escherichia coli (E. coli) for research purposes . The recombinant form is often tagged with a His-tag at the N-terminus to facilitate purification and detection . It is used in various applications, including SDS-PAGE and mass spectrometry (MS), and is typically purified to over 90% purity .

GPx1 plays a vital role in protecting hemoglobin in erythrocytes (red blood cells) from oxidative breakdown . In platelets, it is involved in the metabolism of arachidonic acid, which is essential for the production of signaling molecules called eicosanoids . These functions highlight the enzyme’s importance in maintaining cellular integrity and function under oxidative stress conditions.

The enzyme’s ability to detoxify hydrogen peroxide and lipid peroxides makes it a critical component of the body’s antioxidant defense system. It helps prevent oxidative damage to DNA, proteins, and lipids, which can contribute to various diseases, including cancer . GPx1 is one of the few proteins in higher vertebrates that contain selenocysteine at its active site, which is encoded by the unusual stop codon TGA .

Recombinant Human GPx1 is widely used in research to study its structure, function, and role in oxidative stress. It is also used in high-throughput screening assays to identify potential therapeutic compounds that can modulate its activity .