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The recombinant human GPX4 protein with an N-terminal 6xHis tag is expressed using an E. coli system. The GPX4 gene fragment [29-197aa (U73S)] is co-cloned into an expression plasmid with the tag gene. The recombinant plasmid is introduced into E. coli cells, which are cultured for protein expression. Protein expression is induced by IPTG, and the cells are lysed to release the recombinant GPX4 protein. Protein purification is achieved using Ni-NTA affinity chromatography, where the His tag binds to nickel ions, enabling the selective purification of GPX4. The eluted GPX4 protein is analyzed by SDS-PAGE, revealing a purity of greater than 90%. Human GPX4 is a crucial selenoenzyme that plays a significant role in cellular antioxidant defense mechanisms, particularly in the reduction of lipid hydroperoxides and the maintenance of redox homeostasis. Its unique function as the only known enzyme capable of reducing phospholipid hydroperoxides distinguishes it from other glutathione peroxidases, which primarily target hydrogen peroxide and organic hydroperoxides [1][2]. The enzyme's activity is critically dependent on a selenocysteine residue, which is essential for its catalytic function [3]. GPX4 is involved in regulating ferroptosis [1][4]. The enzyme's ability to mitigate oxidative stress is vital for cell survival, particularly in tissues with high oxidative demands, such as the brain and the gastrointestinal tract [5]. GPX4's role extends beyond mere antioxidant activity. It also participates in signaling pathways that affect cell proliferation and apoptosis. In cancer biology, GPX4 has been identified as a potential therapeutic target, as its inhibition can enhance the efficacy of chemotherapeutic agents like cisplatin by promoting ferroptosis cell death in tumor cells [6]. This dual role of GPX4 in both protecting against oxidative damage and facilitating cell death in cancer cells highlights its importance in both health and disease. References:[1] W. Yang, R. Sriramaratnam, M. Welsch, K. Shimada, R. Skouta, V. Viswanathan, et al. Regulation of ferroptotic cancer cell death by gpx4, Cell, vol. 156, no. 1-2, p. 317-331, 2014. https://doi.org/10.1016/j.cell.2013.12.010[2] J. Angeli, M. Schneider, B. Proneth, Y. Tyurina, V. Tyurin, V. Hammond, et al. Inactivation of the ferroptosis regulator gpx4 triggers acute renal failure in mice, Nature Cell Biology, vol. 16, no. 12, p. 1180-1191, 2014. https://doi.org/10.1038/ncb3064[3] S. Zhu, Q. Zhang, X. Sun, H. Zeh, M. Lotze, R. Kang, et al. Hspa5 regulates ferroptotic cell death in cancer cells, Cancer Research, vol. 77, no. 8, p. 2064-2077, 2017. https://doi.org/10.1158/0008-5472.can-16-1979[4] M. Gaschler, A. Andia, H. Liu, J. Csuka, B. Hurlocker, C. Vaianaet al., Fino2 initiates ferroptosis through gpx4 inactivation and iron oxidation, Nature Chemical Biology, vol. 14, no. 5, p. 507-515, 2018. https://doi.org/10.1038/s41589-018-0031-6[5] B. Speckmann, H. Bidmon, A. Pinto, M. Anlauf, H. Sies, & H. Steinbrenner, Induction of glutathione peroxidase 4 expression during enterocytic cell differentiation, Journal of Biological Chemistry, vol. 286, no. 12, p. 10764-10772, 2011. https://doi.org/10.1074/jbc.m110.216028[6] X. Zhang, S. Sui, L. Wang, H. Li, L. Zhang, S. Xu, et al. Inhibition of tumor propellant glutathione peroxidase 4 induces ferroptosis in cancer cells and enhances anticancer effect of cisplatin, Journal of Cellular Physiology, vol. 235, no. 4, p. 3425-3437, 2019. https://doi.org/10.1002/jcp.29232
The recombinant human GPX4 protein with an N-terminal 6xHis tag is expressed using an E. coli system. The GPX4 gene fragment [29-197aa (U73S)] is co-cloned into an expression plasmid with the tag gene. The recombinant plasmid is introduced into E. coli cells, which are cultured for protein expression. Protein expression is induced by IPTG, and the cells are lysed to release the recombinant GPX4 protein. Protein purification is achieved using Ni-NTA affinity chromatography, where the His tag binds to nickel ions, enabling the selective purification of GPX4. The eluted GPX4 protein is analyzed by SDS-PAGE, revealing a purity of greater than 90%.
Human GPX4 is a crucial selenoenzyme that plays a significant role in cellular antioxidant defense mechanisms, particularly in the reduction of lipid hydroperoxides and the maintenance of redox homeostasis. Its unique function as the only known enzyme capable of reducing phospholipid hydroperoxides distinguishes it from other glutathione peroxidases, which primarily target hydrogen peroxide and organic hydroperoxides [1][2]. The enzyme’s activity is critically dependent on a selenocysteine residue, which is essential for its catalytic function [3].
GPX4 is involved in regulating ferroptosis [1][4]. The enzyme’s ability to mitigate oxidative stress is vital for cell survival, particularly in tissues with high oxidative demands, such as the brain and the gastrointestinal tract [5]. GPX4’s role extends beyond mere antioxidant activity. It also participates in signaling pathways that affect cell proliferation and apoptosis. In cancer biology, GPX4 has been identified as a potential therapeutic target, as its inhibition can enhance the efficacy of chemotherapeutic agents like cisplatin by promoting ferroptosis cell death in tumor cells [6]. This dual role of GPX4 in both protecting against oxidative damage and facilitating cell death in cancer cells highlights its importance in both health and disease.
References:[1] W. Yang, R. Sriramaratnam, M. Welsch, K. Shimada, R. Skouta, V. Viswanathan, et al. Regulation of ferroptotic cancer cell death by gpx4, Cell, vol. 156, no. 1-2, p. 317-331, 2014. https://doi.org/10.1016/j.cell.2013.12.010[2] J. Angeli, M. Schneider, B. Proneth, Y. Tyurina, V. Tyurin, V. Hammond, et al. Inactivation of the ferroptosis regulator gpx4 triggers acute renal failure in mice, Nature Cell Biology, vol. 16, no. 12, p. 1180-1191, 2014. https://doi.org/10.1038/ncb3064[3] S. Zhu, Q. Zhang, X. Sun, H. Zeh, M. Lotze, R. Kang, et al. Hspa5 regulates ferroptotic cell death in cancer cells, Cancer Research, vol. 77, no. 8, p. 2064-2077, 2017. https://doi.org/10.1158/0008-5472.can-16-1979[4] M. Gaschler, A. Andia, H. Liu, J. Csuka, B. Hurlocker, C. Vaianaet al., Fino2 initiates ferroptosis through gpx4 inactivation and iron oxidation, Nature Chemical Biology, vol. 14, no. 5, p. 507-515, 2018. https://doi.org/10.1038/s41589-018-0031-6[5] B. Speckmann, H. Bidmon, A. Pinto, M. Anlauf, H. Sies, & H. Steinbrenner, Induction of glutathione peroxidase 4 expression during enterocytic cell differentiation, Journal of Biological Chemistry, vol. 286, no. 12, p. 10764-10772, 2011. https://doi.org/10.1074/jbc.m110.216028[6] X. Zhang, S. Sui, L. Wang, H. Li, L. Zhang, S. Xu, et al. Inhibition of tumor propellant glutathione peroxidase 4 induces ferroptosis in cancer cells and enhances anticancer effect of cisplatin, Journal of Cellular Physiology, vol. 235, no. 4, p. 3425-3437, 2019. https://doi.org/10.1002/jcp.29232
| Cat.No | ACP01911 | Target Name | GPX4 |
|---|---|---|---|
| Target Synonyms | PHGPx;Glutathione peroxidase 4;GPx-4;GSHPx-4 | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 29-197aa(U73S) |
| Mol Weight | 23.4 kDa | Protein Length | Partial |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P36969 |
|---|
Uniprot Id
P36969
Target Species
Human
Target Name
GPX4
Target Full Name
Phospholipid hydroperoxide glutathione peroxidase GPX4
Target Function
Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide. Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation. Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species. The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis. The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures. May be required to protect cells from the toxicity of ingested lipid hydroperoxides. Required for normal sperm development and male fertility. Essential for maturation and survival of photoreceptor cells. Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion. Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism. Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway.
Target Involvement
Spondylometaphyseal dysplasia, Sedaghatian type (SMDS)
Target Subcellular Location
[Isoform Mitochondrial]: Mitochondrion.; [Isoform Cytoplasmic]: Cytoplasm.
Target Protein Families
Glutathione peroxidase family
Target Tissue Specificity
Present primarily in testis. Expressed in platelets (at protein level).
Target Research Area
Cancer
Target Synonyms
Glutathione peroxidase 4; GPX 4; GPX-4; GPX4; GPX4_HUMAN; GSHPx-4; MCSP; mitochondrial; PHGPx; Phospholipid hydroperoxidase; Phospholipid hydroperoxide glutathione peroxidase; Phospholipid hydroperoxide glutathione peroxidase mitochondrial; snGPx; snPHGPx; Sperm nucleus glutathione peroxidase
Target Background
The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of hydrogen peroxide, organic hydroperoxides and lipid hydroperoxides, and thereby protect cells against oxidative damage. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme has a high preference for lipid hydroperoxides and protects cells against membrane lipid peroxidation and cell death. It is also required for normal sperm development; thus, it has been identified as a 'moonlighting' protein because of its ability to serve dual functions as a peroxidase, as well as a structural protein in mature spermatozoa. Mutations in this gene are associated with Sedaghatian type of spondylometaphyseal dysplasia (SMDS). This isozyme is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Transcript variants resulting from alternative splicing or use of alternate promoters have been described to encode isoforms with different subcellular localization.
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