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The protein encoded by PRDX4 is an antioxidant enzyme and belongs to the peroxiredoxin family. Additionally we are shipping Peroxiredoxin 4 Proteins (22) and Peroxiredoxin 4 Kits (14) and many more products for this protein.
Showing 10 out of 101 products:
Human Polyclonal Peroxiredoxin 4 Primary Antibody for EIA, IHC (p) - ABIN954101
Jamaluddin, Wiktorowicz, Soman, Boldogh, Forbus, Spratt, Garofalo, Brasier: Role of peroxiredoxin 1 and peroxiredoxin 4 in protection of respiratory syncytial virus-induced cysteinyl oxidation of nuclear cytoskeletal proteins. in Journal of virology 2010
Show all 4 references for ABIN954101
Mouse (Murine) Polyclonal Peroxiredoxin 4 Primary Antibody for IHC, WB - ABIN3022012
OFlaherty, de Souza: Hydrogen peroxide modifies human sperm peroxiredoxins in a dose-dependent manner. in Biology of reproduction 2011
Show all 3 references for ABIN3022012
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 (show INS Antibodies) levels and improving the ER folding capacity also under conditions of a high insulin (show INS Antibodies) 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 (show GCLC Antibodies). We reported that the deficiency of antioxidant PRDX4 was associated with pathophysiological mechanism of PCOS.
peroxiredoxin IV recycling in the endoplasmic reticulum is much less efficient than in the cytosol or mitochondria, leading to the protection of peroxiredoxin IV from hyperoxidation.
Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding.
data provide the first evidence of the beneficial effects of PRDX4 on intestinal function in the reduction of the severity of NAFLD (show TSC2 Antibodies), by ameliorating oxidative stress-induced (show SQSTM1 Antibodies) local and systemic injury
The ventral signal observed for Prdx4 from early stages colocalized with motor neuron markers Isl1 (show ISL1 Antibodies)/2 and FoxP1 (show FOXP1 Antibodies) and the strong ventral signal colocalizing with Isl1 (show ISL1 Antibodies)/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 (show GDPD5 Antibodies) enzymatic domain, which blocks GDE2 (show GDPD5 Antibodies) trafficking to the plasma membrane and prevents GDE2 (show GDPD5 Antibodies) neurogeneic function.
PRDX4 may protect against nonalcoholic steatohepatitis and type 2 diabetes by ameliorating oxidative stress-induced (show SQSTM1 Antibodies) 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