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The protein encoded by PRDX4 is an antioxidant enzyme and belongs to the peroxiredoxin family. Zusätzlich bieten wir Ihnen Peroxiredoxin 4 Antikörper (108) und Peroxiredoxin 4 Kits (23) und viele weitere Produktgruppen zu diesem Protein an.
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Human Peroxiredoxin 4 Protein expressed in Escherichia coli (E. coli) - ABIN666967
Jin, Chae, Rhee, Jeang: Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. in The Journal of biological chemistry 1998
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Mouse (Murine) Peroxiredoxin 4 Protein expressed in Escherichia coli (E. coli) - ABIN2121842
Zhao, Du, Zhou, Liu, Gu, Long: Differences in Proinflammatory Property of Six Subtypes of Peroxiredoxins and Anti-Inflammatory Effect of Ligustilide in Macrophages. in PLoS ONE 2016
Results show that ERp44 (zeige ERP44 Proteine) binds the oxidized but not the reduced form of Prx4; the ERp44 (zeige ERP44 Proteine)-Prx4 complex is formed via thiol-disulfide interchange reactions, and its crystal structure reveals a redox-dependent recognition.
Prdx4 expression was closely related to follicular development and has aprominent role in protecting human and mouse granulosa cells from reactive oxygen species damage.
Positive Prx 4 expression is significantly correlated with recurrence and shorter disease-free survival in patients with early-stage lung squamous cell carcinoma.
An off-pathway reaction in the Prx4-mediated oxidative protein folding.
Findings suggest that elevated serum Prx4 levels are associated with a higher risk of incident type 2 diabetes
Prx4 is a circulating antioxidant and is independently associated with increased risk of cardiovascular and all-cause mortality in T2DM.
these data suggest an important role of Prdx4 in maintaining insulin (zeige INS Proteine) levels and improving the ER folding capacity also under conditions of a high insulin (zeige INS Proteine) requirement.
there is a significant difference in concentration of Prx4 between cardiac arrest patients with good and poor outcome
The structure and function of PRDX4 as well as its sensitivity to hyperoxidation. [Review]
expression of PRDX4 in PCOS ovaries appeared to be mediated through oxidative stress in GCs (zeige GCLC Proteine). We reported that the deficiency of antioxidant PRDX4 was associated with pathophysiological mechanism of PCOS.
data provide the first evidence of the beneficial effects of PRDX4 on intestinal function in the reduction of the severity of NAFLD, by ameliorating oxidative stress-induced (zeige SQSTM1 Proteine) local and systemic injury
The ventral signal observed for Prdx4 from early stages colocalized with motor neuron markers Isl1 (zeige ISL1 Proteine)/2 and FoxP1 (zeige FOXP1 Proteine) and the strong ventral signal colocalizing with Isl1 (zeige ISL1 Proteine)/2 was observed in all rostrocaudal segments of the spinal cord.
Prdx4 dimers generated by hydrogen peroxide metabolism oxidize two cysteine residues within the GDE2 (zeige GDPD5 Proteine) enzymatic domain, which blocks GDE2 (zeige GDPD5 Proteine) trafficking to the plasma membrane and prevents GDE2 (zeige GDPD5 Proteine) neurogeneic function.
PRDX4 may protect against nonalcoholic steatohepatitis and type 2 diabetes by ameliorating oxidative stress-induced (zeige SQSTM1 Proteine) injury.
data suggest that PRDX4 can be a novel target for glioblastoma multiforme therapies in the future
combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta, and PRDX4 compromised the extracellular matrix and interfered with the intracellular maturation of procollagen
Prx IV-L functions as an H(2)O(2) sensor that mediates protein thiol oxidation required for the maturation of spermatozoa in placental mammals.
The results indicate that spermatogenic cells lacking Prx4 are more susceptible to cell death via oxidative damage than their wild-type counterparts.
The protein encoded by this gene is an antioxidant enzyme and belongs to the peroxiredoxin family. The protein is localized to the cytoplasm. Peroxidases of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. This protein has been found to play a regulatory role in the activation of the transcription factor NF-kappaB.
, thioredoxin peroxidase
, antioxidant enzyme AOE372
, peroxiredoxin IV
, thioredoxin peroxidase (antioxidant enzyme)
, thioredoxin peroxidase AO372
, thioredoxin-dependent peroxide reductase A0372
, Prx IV