Active • Host: E. coli strain C321.ΔA.exp • AA: 1-170 (full length) • Tag: N-terminal His • MW: 21.2 kDa
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GPX4 (human, recombinant; His-tagged)

Item No. 26906

Technical Information
Synonyms
  • Glutathione Peroxidase 4
  • PHGPx
  • Phospholipid Hydroperoxide Glutathione Peroxidase
Purity
≥80% estimated by SDS-PAGE
Source
Active recombinant N-terminal His-tagged protein expressed in E. coli strain C321.ΔA.exp
Amino Acids
1-170 (full length)
MW
21.2 kDa
50 mM potassium phosphate buffer, pH 7.6, with 0.1 mM DTT and 5% glycerol
UniProt Accession №
P36969-2
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    Product Description

    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 (human, recombinant; His-tagged) protein has a selenocysteine incorporated in the active site that has been confirmed by mass spectrometry. It can be used for Western blot, ELISA, and enzymatic assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Imai, H., and Nakagawa, Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 34(2), 145-169 (2003).

    2. Forcina, G.C., and Dixon, S.J. GPX4 at the crossroads of lipid homeostasis and ferroptosis. Proteomics 19(18), e1800311 (2019).

    3. Maiorino, M., Scapin, M., Ursin, F., et alDistinct promoters determine alternative transcription of gpx-4 into phospholipid-hydroperoxide glutathione peroxidase variants. The Journal of Biological Chemisty 278(36), 34286-34290 (2003).

    4. Smith, A.C., Mears, A.J., Bunker, R., et alMutations in the enzyme glutathione peroxidase 4 cause Sedaghatian-type spondylometaphyseal dysplasia. J. Med. Genet. 51(7), 470-474 (2014).

    Product Citations

    Xue, Q., Yan, D., Chen, X., et alCopper-dependent autophagic degradation of GPX4 drives ferroptosis. Autophagy (2023).