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PRDX2 encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. Additionally we are shipping Peroxiredoxin 2 Kits (36) and Peroxiredoxin 2 Proteins (31) and many more products for this protein.
Showing 10 out of 146 products:
Human Monoclonal Peroxiredoxin 2 Primary Antibody for IF, IHC (p) - ABIN563132
Desmetz, Bascoul-Mollevi, Rochaix, Lamy, Kramar, Rouanet, Maudelonde, Mangé, Solassol: Identification of a new panel of serum autoantibodies associated with the presence of in situ carcinoma of the breast in younger women. in Clinical cancer research : an official journal of the American Association for Cancer Research 2009
Show all 2 references for ABIN563132
Cow (Bovine) Polyclonal Peroxiredoxin 2 Primary Antibody for IHC, WB - ABIN2783315
Fang, Nakamura, Cho, Gu, Lipton: S-nitrosylation of peroxiredoxin 2 promotes oxidative stress-induced neuronal cell death in Parkinson's disease. in Proceedings of the National Academy of Sciences of the United States of America 2007
Human Polyclonal Peroxiredoxin 2 Primary Antibody for EIA, WB - ABIN374698
Kato, Kato, Abe, Matsumura, Nishino, Aoki, Itoyama, Asayama, Awaya, Hirano, Ohama et al.: Redox system expression in the motor neurons in amyotrophic lateral sclerosis (ALS): immunohistochemical studies on sporadic ALS, superoxide dismutase 1 (SOD1)-mutated familial ALS, and SOD1-mutated ... in Acta neuropathologica 2005
Prx1 (show PRDX1 Antibodies) and Prx2 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 indicate that peroxiredoxin 2 (PRDX2) was upregulated in white matter multiple sclerosis (MS) lesions mainly in astrocytes, and its expression level was positively correlated with the degree of inflammation and oxidative stress, and suggest that PRDX2 expression contributes to the resistance of astrocytes against oxidative damage.
The levels of expression of carbonic anhydrase 2 (show CA2 Antibodies), catalase (show CAT Antibodies), and PRDX2 in the nipple discharge were significantly increased in breast ductal carcinoma patients as compared to controls.
Activation of PRX1 (show PRDX1 Antibodies) and -2 indicate cold atmospheric plasma affects redox homeostasis in osteosarcoma cells
ig-h3, Peroxiredoxin-2, and NRF2 (show GABPA Antibodies) have roles in cervical carcinogenesis
Data show that peroxiredoxins PRDX1 (show PRDX1 Antibodies) and PRDX2 are upregulated in tumor B cells as compared with normal counterparts.
Data show the protein partners of human Prx1 (show PRDX1 Antibodies) and Prx2 and identified three sequence motifs, or combination thereof in Prxs partners, namely: CXXC, PXXP, and LXXLL. that can be important for protein localization, function and biological pathways. [review]
Oxidative stress promotes PRX2 and PRX3 (show PRDX3 Antibodies) hyperoxidation and attenuates pro-survival signaling in aging chondrocytes.
Prx2 glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 (show GRX1 Antibodies) provide an alternative mechanism to thioredoxin (show TXN Antibodies) and thioredoxin reductase (show PRDX5 Antibodies) for Prx2 recycling.
the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3 (show PRDX3 Antibodies). Reduction and re-oxidation of the hyperoxidized dimer of Prx3 (show PRDX3 Antibodies) produced hyperoxidized monomers
Oxidative stress promotes PRX2 (show PRRX2 Antibodies) and PRX3 (show PRDX3 Antibodies) hyperoxidation and attenuates pro-survival signaling in aging chondrocytes.
The ventral signal observed for Prdx2 from early stages colocalized with motor neuron markers Isl1 (show ISL1 Antibodies)/2 and FoxP1 (show FOXP1 Antibodies) and strong ventral signal colocalizing with Isl1 (show ISL1 Antibodies)/2 was observed in all rostrocaudal segments of the spinal cord.
Prx2 (show PRRX2 Antibodies) glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 (show GRX1 Antibodies) provide an alternative mechanism to thioredoxin (show TXN Antibodies) and thioredoxin reductase for Prx2 (show PRRX2 Antibodies) recycling.
elevation in hyperoxidized Prxs, notably Prx2 (show PRRX2 Antibodies) and Prx3 (show PRDX3 Antibodies), was observed in several organs from SOD1 (show SOD1 Antibodies)-deficient mice. However, a SOD1 (show SOD1 Antibodies) deficiency had no impact on the wheel-running activity of the mice
PrxII functions as a protective antioxidant enzyme against collagen-stimulated platelet activation and platelet-dependent thrombosis
Prx I and Prx II appear to have a tight association with the mechanism underlying the protection of ESC stemness in developing teratomas.
results suggest that inactivation of PrxII is important for the stability of FoxO1 (show FOXO1 Antibodies) protein, which subsequently mediates Foxp3 (show FOXP3 Antibodies)( ) Treg cell development, thereby attenuating colonic inflammation
PRDX2 neutralizes hydrogen peroxide generated in vivo under the transient hypoxic conditions experienced as erythrocytes pass through the microcirculation.
PRX2 (show PRRX2 Antibodies) battles poly(ADP-ribose) polymerase 1 (show PARP1 Antibodies)- and p53 (show TP53 Antibodies)-dependent prodeath pathways after ischemic injury
These findings suggest that Prx (show PRX Antibodies) II plays an important role in preventing hemolytic anemia from oxidative stress by binding to Hb as a decameric structure to stabilize it.
This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein plays an antioxidant protective role in cells, and it may contribute to the antiviral activity of CD8(+) T-cells. The crystal structure of this protein has been resolved to 2.7 angstroms. This protein prevents hemolytic anemia from oxidative stress by stabilizing hemoglobin, thus making this gene a therapeutic target for patients with hemolytic anemia. This protein may have a proliferative effect and play a role in cancer development or progression. Related pseudogenes have been identified on chromosomes 5, 6, 10 and 13.
natural killer cell-enhancing factor B
, thiol-specific antioxidant 1
, thioredoxin peroxidase 1
, thioredoxin-dependent peroxide reductase 1
, Prx II-1
, Trx dependent peroxide reductase 1
, protector protein
, thiol specific antioxidant protein
, thiol-specific antioxidant protein
, thioredoxin dependent peroxide reductase 1
, thioredoxin reductase