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GLRX encodes a member of the glutaredoxin family. Additionally we are shipping Glutaredoxin Antibodies (26) and Glutaredoxin Kits (4) and many more products for this protein.
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Glrx (show GRX1 Proteins) ablation stabilizes HIF-1alpha (show HIF1A Proteins) by increasing GSH adducts on Cys (show DNAJC5 Proteins)(520) promoting in vivo HIF-1alpha (show HIF1A Proteins) stabilization, VEGF-A (show VEGFA Proteins) production, and revascularization in the ischemic muscles.
Prx2 (show PRRX2 Proteins) 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 Proteins) provide an alternative mechanism to thioredoxin (show TXN Proteins) and thioredoxin reductase (show PRDX2 Proteins) for Prx2 (show PRRX2 Proteins) recycling.
The temporal relationships of Glrx1 (show GRX1 Proteins) with protein S-glutathionylation, glutathione, and cytokines/chemokines were observed as dynamic changes in lungs with allergic airway inflammation
Glutaredoxin 1 (show GRX1 Proteins) plays an important role in controlling epithelial cell responsiveness to IL-17A (show IL17A Proteins)
Up-r (show GRX1 Proteins)egulated Glrx inhibits VEGF signaling by increa (show FLT1 Proteins)sed Flt1 causing impaired vascularization.
S-glutathionylation of Fas (show FAS Proteins) in lung epithelium enhances epithelial apoptosis and clearance of P. aeruginosa. Glutaredoxin-1 (show GRX1 Proteins) impairs bacterial clearance and increases severity of pneumonia in association with deglutathionylation of Fas (show FAS Proteins).
These data suggest that the overexpression of GRX1 (show GRX1 Proteins) could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH (show GAPDH Proteins).
we provide evidence that Grx1 (show GRX1 Proteins) has an important role in regulating cigarette smoke-induced lung inflammation which seems to diverge from its effects on total PSSG.
Data show that glutaredoxin (show GRX1 Proteins) acts as a reductant for methionine sulfoxide reductases A and B (MsrA (show MSR1 Proteins) and MsrB (show MSRB2 Proteins)) with or without resolving cysteine.
results are the first to demonstrate that Grx-1 (show GRX1 Proteins) induces angiogenesis and diminishes ventricular remodeling apparently through neovascularization mediated by Akt (show AKT1 Proteins), VEGF (show VEGFA Proteins), Ang-1 (show ANGPT1 Proteins) and NF-kappaB (show NFKB1 Proteins) as well as Bcl-2 (show BCL2 Proteins) and survivin (show BIRC5 Proteins)-mediated anti-apoptotic pathway
The results demonstrate that the antiproliferative effect of NO is hampered by Trx1 (show MLL Proteins) and Grx1 (show GRX1 Proteins) and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Prx2 (show PRDX2 Proteins) 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 Proteins) provide an alternative mechanism to thioredoxin (show TXN Proteins) and thioredoxin reductase (show PRDX5 Proteins) for Prx2 (show PRDX2 Proteins) recycling.
Glutaredoxin 1 (show GRX1 Proteins) protects human retinal pigment epithelial cells from oxidative damage by preventing AKT (show AKT1 Proteins) glutathionylation.
A new function for GRX1 (show GRX1 Proteins) in neuronal copper homeostasis and in protection from copper-mediated oxidative injury.
Human Grx1 (show GRX1 Proteins) can catalyse reduction of Atox1 (show ATOX1 Proteins) by glutathione but only in the presence of Cu(I).
Levels of GLRX (show GRX1 Proteins) in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease.
Glrx (show GRX1 Proteins) overexpression increased soluble VEGF receptor (show FLT1 Proteins) 1 (sFlt) in endothelial cells via NF-kappaB (show NFKB1 Proteins)-dependent Wnt5a (show WNT5A Proteins) production.
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin (show GRX1 Proteins) system.
sputum glutaredoxin-1 (show GRX1 Proteins) may have a role in asthma, while protein S may have a role in better lung function
This gene encodes a member of the glutaredoxin family. The encoded protein is a cytoplasmic enzyme catalyzing the reversible reduction of glutathione-protein mixed disulfides. This enzyme highly contributes to the antioxidant defense system. It is crucial for several signalling pathways by controlling the S-glutathionylation status of signalling mediators. It is involved in beta-amyloid toxicity and Alzheimer's disease. Multiple alternatively spliced transcript variants encoding the same protein have been identified.
, glutaredoxin (thioltransferase)
, glutaredoxin 1 (thioltransferase)