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catalyzes the deglutathionylation of protein-SS-glutathione mixed disulfides. Additionally we are shipping Glutaredoxin Proteins (10) and Glutaredoxin Kits (6) and many more products for this protein.
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Glrx (show GRX1 Antibodies) ablation stabilizes HIF-1alpha (show HIF1A Antibodies) by increasing GSH adducts on Cys (show DNAJC5 Antibodies)(520) promoting in vivo HIF-1alpha (show HIF1A Antibodies) stabilization, VEGF-A (show VEGFA Antibodies) production, and revascularization in the ischemic muscles.
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 (show PRDX2 Antibodies) for Prx2 (show PRRX2 Antibodies) recycling.
The temporal relationships of Glrx1 (show GRX1 Antibodies) with protein S-glutathionylation, glutathione, and cytokines/chemokines were observed as dynamic changes in lungs with allergic airway inflammation
Glutaredoxin 1 (show GRX1 Antibodies) plays an important role in controlling epithelial cell responsiveness to IL-17A (show IL17A Antibodies)
Up-r (show GRX1 Antibodies)egulated Glrx inhibits VEGF signaling by increa (show FLT1 Antibodies)sed Flt1 causing impaired vascularization.
S-glutathionylation of Fas (show FAS Antibodies) in lung epithelium enhances epithelial apoptosis and clearance of P. aeruginosa. Glutaredoxin-1 (show GRX1 Antibodies) impairs bacterial clearance and increases severity of pneumonia in association with deglutathionylation of Fas (show FAS Antibodies).
These data suggest that the overexpression of GRX1 (show GRX1 Antibodies) could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH (show GAPDH Antibodies).
we provide evidence that Grx1 (show GRX1 Antibodies) 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 Antibodies) acts as a reductant for methionine sulfoxide reductases A and B (MsrA (show MSR1 Antibodies) and MsrB (show MSRB2 Antibodies)) with or without resolving cysteine.
results are the first to demonstrate that Grx-1 (show GRX1 Antibodies) induces angiogenesis and diminishes ventricular remodeling apparently through neovascularization mediated by Akt (show AKT1 Antibodies), VEGF (show VEGFA Antibodies), Ang-1 (show ANGPT1 Antibodies) and NF-kappaB (show NFKB1 Antibodies) as well as Bcl-2 (show BCL2 Antibodies) and survivin (show BIRC5 Antibodies)-mediated anti-apoptotic pathway
Glutaredoxin (show GRX1 Antibodies) desensitizes lens to oxidative stress by connecting and integrating specific signaling and transcriptional regulation for antioxidant response.
The results demonstrate that the antiproliferative effect of NO is hampered by Trx1 (show MLL Antibodies) and Grx1 (show GRX1 Antibodies) and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Prx2 (show PRDX2 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 (show PRDX5 Antibodies) for Prx2 (show PRDX2 Antibodies) recycling.
Glutaredoxin 1 (show GRX1 Antibodies) protects human retinal pigment epithelial cells from oxidative damage by preventing AKT (show AKT1 Antibodies) glutathionylation.
A new function for GRX1 (show GRX1 Antibodies) in neuronal copper homeostasis and in protection from copper-mediated oxidative injury.
Human Grx1 (show GRX1 Antibodies) can catalyse reduction of Atox1 (show ATOX1 Antibodies) by glutathione but only in the presence of Cu(I).
Levels of GLRX (show GRX1 Antibodies) in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease.
Glrx (show GRX1 Antibodies) overexpression increased soluble VEGF receptor (show FLT1 Antibodies) 1 (sFlt) in endothelial cells via NF-kappaB (show NFKB1 Antibodies)-dependent Wnt5a (show WNT5A Antibodies) production.
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin (show GRX1 Antibodies) system.
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)