Recombinant Human Peroxiredoxin 4 protein is a Human Full Length protein, in the 38 to 271 aa range, expressed in Escherichia coli, with >95%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE.
대체 명칭 보기
Peroxiredoxin-4, Antioxidant enzyme AOE372, Peroxiredoxin IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Thioredoxin-dependent peroxiredoxin 4, AOE37-2, Prx-IV, PRDX4
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Peroxiredoxin 4 protein (AB172175)
SDS-PAGE gel showing ab172175 under non-reduced (Lane 1) and reduced (Lane 2) conditions.
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Prdx4 plays a list of roles in cellular defense against oxidative stress. It not only reduces peroxides but also contributes to the maintenance of protein folding by modifying disulfide bonds in the endoplasmic reticulum. Prdx4 does not function as part of a larger complex but acts independently within its compartments. The protective functions of Prdx4 are important for cell survival and proper cellular function.
Pathways
Prdx4 interacts with oxidative stress response pathways. Specifically it participates in the redox signaling pathways that regulate cellular reactive oxygen species levels. Peroxiredoxin 4 is closely associated with proteins such as thioredoxin in these pathways. Together they regulate the cellular redox environment which is important for maintaining cellular homeostasis.
일반 정보
기능
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
서열 유사성
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Post-translational modifications
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond.
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