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Glutathione peroxidase 4 (GPX4) is a selenocysteine-containing glutathione peroxidase that is encoded by the GPX4 gene in humans and protects cellular membranes from oxidative damage.1,2 It is a monomeric protein consisting of a thioredoxin motif and a selenocysteine-glutamine-tryptophan catalytic triad that reduces lipid hydroperoxides, including phospholipid, polyunsaturated lipid, and sterol hydroperoxides, to non-toxic lipid alcohols. During this process, the active site selenocysteine becomes oxidized and must subsequently be replenished by the reducing substrate glutathione (GSH).2 There are three isoforms of GPX4, mitochondrial mGPX4, cytosolic cGPX4, and nuclear nGPX4/snGPX4, that are expressed in all tissue types in rats, with the highest mRNA levels observed in testes.1,2,3 GPX4 is a key regulator of ferroptosis that inhibits ferroptotic cell death by preventing iron-dependent accumulation of toxic lipid reactive oxygen species.2 Mutations in GPX4 have been found in patients with Sedaghatian-type spondylometaphyseal dysplasia (SSMD), and silencing of Gpx4 in mice is embryonic lethal.4,2 Cayman's GPX4 Polyclonal Antibody can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes GPX4 at 20 kDa from human, mouse, rat, and porcine samples.
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1. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 34(2), 145-169 (2003).
2. GPX4 at the crossroads of lipid homeostasis and ferroptosis. Proteomics 19(18), e1800311 (2019).
3. Distinct promoters determine alternative transcription of gpx-
4. Mutations in the enzyme glutathione peroxidase 4 cause Sedaghatian-
Impact of glutathione peroxidase 4 on cell proliferation, angiogenesis and cytokine production in hepatocellular carcinoma. Oncotarget 9(11), 10054-10068 (2018).