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anti-Mouse (Murine) Glutathione Reductase Antibodies:
anti-Rat (Rattus) Glutathione Reductase Antibodies:
anti-Human Glutathione Reductase Antibodies:
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Arabidopsis thaliana Polyclonal Glutathione Reductase Primary Antibody for IL, IP - ABIN190699
Sobrino-Plata, Ortega-Villasante, Flores-Cuaceres, Escobar, Del Campo, Hernuandez: Differential alterations of antioxidant defenses as bioindicators of mercury and cadmium toxicity in alfalfa. in Chemosphere 2009
Show all 4 Pubmed References
Human Polyclonal Glutathione Reductase Primary Antibody for WB - ABIN4314709
Yang, Yang, Cao: Acetyl-l-carnitine prevents homocysteine-induced suppression of Nrf2/Keap1 mediated antioxidation in human lens epithelial cells. in Molecular medicine reports 2015
Schistosoma mansoni Polyclonal Glutathione Reductase Primary Antibody for IHC - ABIN966206
Berriman, Haas, LoVerde, Wilson, Dillon, Cerqueira, Mashiyama, Al-Lazikani, Andrade, Ashton, Aslett, Bartholomeu, Blandin, Caffrey, Coghlan, Coulson, Day, Delcher, DeMarco, Djikeng, Eyre, Gamble, Ghedin, Gu, Hertz-Fowler, Hirai, Hirai, Houston, Ivens, Joh: The genome of the blood fluke Schistosoma mansoni. in Nature 2009
Data indicate that glutathione reductase 2 (GR2) protects photosystem II (PSII) from excess light and maintains the function of acceptor side of PSII.
Plastid-localized glutathione reductase-2-regulated glutathione redox status is essential for Arabidopsis root apical meristem maintenance.
GSR is not essential for the maintenance of antioxidant defenses in mouse cochlea; the thioredoxin/thioredoxin (show TXN Antibodies) reductase (show PRDX2 Antibodies) system can probably operate as a functional backup for GSR.
Data show that reducing RGS2 (show RGS2 Antibodies) expression by antisense treatment prevented the increase in GLO1 (show GLO1 Antibodies) and GSR1 mRNA and protein expression.
Local overexpression in the mouse brain resulted in increased anxiety-like behaviour; Gsr is involved in oxidative stress metabolism, linking this pathway with anxiety-related behaviour
Liver biopsy is a valuable tool for detecting oxidative stress and for diagnosing hepatic dysfunction in cattle from glutathione and glutathione reductase levels.
It has been shown that acute aerobic exercise activates Nrf2 (show GABPA Antibodies) in young men, irrespective of training intensity, but that high-intensity exercise demonstrated a greater effect on increasing glutathione reductase activity which could indicate improved redox potential.
GSR expression was higher in TMZ-resistant cells than in sensitive cells. GSR silencing in drug-resistant cells improved the sensitivity of cells to TMZ or cisplatin. Over-expression resulted in resistance. GSR partially prevented the oxidative stress caused by L-buthionine -sulfoximine. The action of GSR in drug resistance is associated with the modulation of redox homeostasis. High GSR correlated with lower survival.
Plasma glutathione reductase (GR) activity was correlated with erythrocyte GR activity and the erythrocyte reduced glutathione/glutathione disulfide ratio. A decrease in plasma GR activity was associated with an increase in mortality in septic shock.
Glutathione reductase reduces mitochondrial protein (show COX6B2 Antibodies) mitoNEET (show CISD1 Antibodies) [2Fe-2S] clusters.
The recurrence of benign tumors of mammary gland occurred predominantly in women-carriers of mutant alleles with polymorphism rs8190924 of gene GSR and AA rs3763511of gene DKK4 (show DKK4 Antibodies).
GSR was the most significant single SNP association with systemic lupus erythematosus in African Americans.
1,25 (OH) vitamin D significantly upregulated expression of GCLC (show GCLC Antibodies) and GR and lowered secretion of IL-8 (show IL8 Antibodies) and MCP-1 (show CCL2 Antibodies) in high-glucose exposed U937 monocytes.
The results demonstrate for the first time that glutathione reductase gene polymorphisms are significantly associated with bone mineral density.
Up-regulation of CAT and GR activity resulted in an increase in total antioxidant activity in A549 after exposure to B (show TDO2 Antibodies)(a)P.
Human eye lenses were dissected into discrete regions that were formed at different stages of life and assayed for activity of lactate dehydrogenase (LDH) and a particularly stable enzyme, glutathione reductase (GR).
Overexpression of mitochondrial TXNRD2 (show TXNRD2 Antibodies) in Drosophila melanogaster extended median lifespan in female flies with a small lifespan extension in males; in contrast, overexpression of the cytosolic form, TXNRD1 (show TXNRD1 Antibodies), did not produce a lifespan extension.
Molecular orbital calculations suggested that the C-terminal hexapeptide Pro-Ala-Ser (show SIGLEC1 Antibodies)-Cys-Cys (show DNAJC5 Antibodies)-Ser (show SIGLEC1 Antibodies)-OH functions as a redox center that alleviates the necessity for selenium in Dm-TrxR.
analysis of the mechanism of high Mr thioredoxin reductase from Drosophila melanogaster
changing of His106 to asparagine, glutamine, and phenylalanine in various C-terminal mutants of Drosophila melanogaster thioredoxin reductase drops catalytic activity without change in pH profile
X-ray crystal structure of thioredoxin reductase at 2.4 A resolution; demonstrated that tetrapeptides equivalent to the oxidized C-terminal active sites of both mouse mitochondrial TR (mTR3 (show EXOSC6 Antibodies)) and DmTR are substrates for the truncated forms of both enzymes
redox potentials provide direct evidence for proposed catalytic mechanism of DmTrxR, & cast new light on essential role of DmTrx system in cycling GSSG/GSH & maintaining intracellular redox homeostasis in D. melanogaster without glutathione reductase.
rates of steps in both the reductive and the oxidative half-reactions are markedly diminished in H464'Q thioredoxin reductase as compared to those of wild-type enzyme, indicating that His-464' is involved in both half-reactions
the role of Glu (show SLC2A1 Antibodies)-469' in catalysis by DmTrxR
This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found.
glutathione reductase, gro-2
, glutathione reductase
, glutathione reductase, mitochondrial
, glutathione reductase 1
, glutathione-disulfide reductase
, Glutathione reductase (GR) (GRase)
, disulfide reductase
, thioredoxin reductase
, thioredoxin reductase-1