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Prx1 might play an oncogenic role in tobacco-related oral squamous cell carcinoma and thus serve as a target for chemopreventive and therapeutic interventions.
PRDX1 safeguards telomeres from oxygen radicals to counteract telomere damage and preserve telomeric DNA for elongation by telomerase.
infection results in S-nitrosylation of multiple host proteins, including Prx1.
circulating Prdx1 provides not only prognostic information but may be a promising target against ischemia/reperfusion injury.
our findings suggest that the tumor suppressor activity of SIRT2 (show SIRT2 Proteins) requires its ability to restrict the antioxidant activity of Prdx-1, thereby sensitizing breast cancer cells to reactive oxygen species -induced DNA damage and cell cytotoxicity
The gene signature of OPA1 (show OPA1 Proteins), CTSA (show CTSA Proteins), NDUFA1 (show NDUFA1 Proteins), STK10 (show STK10 Proteins) and PRDX1 was able to identify patients post-implant with a sensitivity of 91% and a specificity of 86% in discrimination between post-implant group and healthy controls.
UV-vis spectra of heme-PRX1 suggested that Cys52 is the axial ligand of ferric heme. PRX1 peroxidase activity was lost upon heme binding, reflecting the fact that Cys52 is not only the heme-binding site but also the active center of peroxidase activity.
Prx1 and Prx2 (show PRDX2 Proteins) are likely targets of urate hydroperoxide in cells. Oxidation of Prxs by urate hydroperoxide might affect cell function and be partially responsible for the pro-oxidant and pro-inflammatory effects of uric acid.
Data suggest that PRX1 is a dual-function enzyme exhibiting both thioredoxin peroxidase (show PER1 Proteins)-like activity and catalase (show CAT Proteins)-like activity with varied affinities towards reactive oxygen species; studies were conducted using recombinant proteins from green spotted puffer fish Tetraodon nigroviridis and from human.
peroxiredoxin 1 has a role in redox sensing and transducing [review]
This is the first report proclaiming that the ESAT-6 regulates Prdx-1 which is involved in the increase of mycobacterial uptake and survival. The intermediate mechanisms involve the increased Prdx-1 production in macrophages through the activation of p38 (show CRK Proteins) and NRF-2 (show NFE2L2 Proteins) dependent signaling.
in the absence of PAG, Csk becomes more associated with alternative partners; i.e., phosphatase PTPN22 and Dok adaptors. Combining PAG deficiency with PTPN22 or Dok adaptor deficiency further enhances effector T cell responses. Unlike PAG, Cbl ubiquitin ligases inhibit the activation of naive, but not of effector, T cells.
These findings suggest that extracellular Prx1-mediated TLR4 (show TLR4 Proteins)/NF-kappaB (show NFKB1 Proteins) pathway activation probably contributes to neuroinflammatory injury after ICH (show ACE Proteins), and thus blocking Prx1-TLR4 (show TLR4 Proteins) signaling might provide a novel anti-neuroinflammatory strategy with extended therapeutic window for hemorrhagic stroke
This study demonstrated that Prdx1 showed a distinct nuclear localization in the spinal cord also present in the nucleus of dorsal root ganglia (DRG) cells as well as in the sensory nerve root in embryonic development.
Prx I and Prx II appear to have a tight association with the mechanism underlying the protection of ESC stemness in developing teratomas.
Prx (show PRX Proteins) I is an antioxidant that is up-regulated in a reactive oxygen species/p38 MAPK (show MAPK14 Proteins)-dependent manner and governs the progression of neuroinflammation by suppressing microglial activation.
NO/SNO donors such as S-nitrosocysteine and S-nitrosoglutathione readily induced the S-nitrosylation of Prx1, causing structural and functional alterations
PrxI is not an effective protector against ozone-induced oxidative damage but plays a positive role in the initiation of lung inflammation following exposure.
Peroxiredoxin 1 stimulates endothelial cell expression of VEGF (show VEGFA Proteins) via TLR4 (show TLR4 Proteins) dependent activation of HIF-1alpha (show HIF1A Proteins).
The clearance rate of Heinz body-containing RBCs (show SSU1 Proteins) in peroxiredoxin I(-/-) mice decreased significantly through the treatment of aniline hydrochloride (AH) compared with wild-type mice.
These results suggest that PRX 1 is a novel mechanosensitive antioxidant, playing an important role in shear-dependent regulation of endothelial biology and atherosclerosis.
It was assumed that Prx1 plays a leading role in X. laevis early development.
The results suggested that scarless skin-wound healing may require activation of the prx1 limb enhancer, and competence to activate the enhancer is probably a prerequisite for epimorphic regeneration, such as limb regeneration.
an IAP (show CD47 Proteins) antagonist that promotes cell death by liberating Dronc from DIAP1 (show DIAPH1 Proteins)
Data suggest a role for peroxiredoxin1 (Prdx1) in vasculature and indicating that the antioxidant function of prdx1 is important.
This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Four transcript variants encoding the same protein have been identified for this gene.
natural killer cell-enhancing factor A
, natural killer-enhancing factor A
, proliferation-associated gene A
, proliferation-associated gene protein
, thioredoxin peroxidase 2
, thioredoxin-dependent peroxide reductase 2
, Trx dependent peroxide reductase 2
, macrophage 23 Kd stress protein
, macrophage 23 kDa stress protein
, macrophage 23kDa stress protein
, macrophase stress protein 22kDa
, macrophase stress protein 23 kd
, osteoblast specific factor 3
, osteoblast-specific factor 3
, thioredoxin dependent peroxide reductase 2
, heme-binding 23 kDa protein
, peroxiredoxin 1
, Thioredoxin peroxidase 2
, thioredoxin peroxidase II