Analytical Data
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Gene name
GPX4
- Application
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Alternative Names
GPX4；Phospholipid hydroperoxide glutathione peroxidase GPX4
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Species
Human
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Source
E. coli
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Tag
N-terminal His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P36969
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Expression Region
29-197aa
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AA Sequence
CASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQSGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRYGPMEEPLVIEKDLPHYF
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Molecular Weight
25.6kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
Glutathione peroxidase 4 (GPX4) is a crucial antioxidant enzyme that plays a significant role in protecting cells from oxidative damage by reducing lipid hydroperoxides to their corresponding alcohols. It is unique among the family of glutathione peroxidases due to its specific ability to reduce lipid peroxides, which are a key contributor to ferroptosis, a form of programmed cell death associated with iron-dependent lipid peroxidation. The study of GPX4 has gained prominence due to its implications in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders. In cancer, GPX4 is often upregulated, contributing to the survival of tumor cells under oxidative stress, thereby presenting a potential target for therapeutic intervention. Research also highlights the relevance of GPX4 in the regulation of ferroptosis, suggesting that manipulating its expression or activity may provide new strategies for treating diseases characterized by dysregulated cell death. Furthermore, studying GPX4 offers insights into the interplay between oxidative stress and metabolism, shedding light on how cells adapt to both oxidative challenges and metabolic demands. Overall, GPX4 represents a promising research focus with the potential to elucidate mechanisms of disease progression and to develop novel therapeutic approaches.
