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AtGRXcp has a glutaredoxin/thioredoxin-like (show TXN ELISA Kits) fold with distinct structural features that differ from those of dithiol glutaredoxins.
Results describe the initial functional characterization of a plant monothiol Glutaredoxin and suggests a conserved biological function in protecting cells against protein oxidative damage [AtGRXcp].
Grx1 deficiency leads to eNOS (show NOS3 ELISA Kits) dysfunction through oxidative modification of S-glutathionylation of eNOS (eNOS (show NOS3 ELISA Kits)-SSG) and inactivation of NO production, enhancing the endothelial TLR4 (show TLR4 ELISA Kits) activation, and ultimately exacerbating necrotizing enterocolitis severity.
Study reports a decrease of Grx expression levels in pancreatic islets of diabetic mice which was accompanied by declining insulin (show INS ELISA Kits) secretion, increase of reactive oxygen species (ROS (show ROS1 ELISA Kits)) production level, and cell cycle alterations. These data demonstrate the essential role of the Grx system for the beta-cell during metabolic stress which may provide a new target for diabetes mellitus type 2 treatment.
Our results indicate that Grx1 upregulation promotes neuroinflammation and consequent neuronal cell death in vitro, and synergizes with proinflammatory insults to promote DA loss in vivo.
the Glrx1-Protein S-glutathionylation axis plays a pivotal role in house dust mite-induced allergic airways disease.
Glrx ablation stabilizes HIF-1alpha (show HIF1A ELISA Kits) by increasing GSH adducts on Cys (show DNAJC5 ELISA Kits)(520) promoting in vivo HIF-1alpha (show HIF1A ELISA Kits) stabilization, VEGF-A (show VEGFA ELISA Kits) production, and revascularization in the ischemic muscles.
Prx2 (show PRRX2 ELISA Kits) glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 provide an alternative mechanism to thioredoxin (show TXN ELISA Kits) and thioredoxin reductase (show PRDX2 ELISA Kits) for Prx2 (show PRRX2 ELISA Kits) recycling.
The temporal relationships of Glrx1 with protein S-glutathionylation, glutathione, and cytokines/chemokines were observed as dynamic changes in lungs with allergic airway inflammation
Glutaredoxin 1 plays an important role in controlling epithelial cell responsiveness to IL-17A (show IL17A ELISA Kits)
Up-regulated Glrx inhibits VEGF signaling by increa (show FLT1 ELISA Kits)sed Flt1 causing impaired vascularization.
S-glutathionylation of Fas (show FAS ELISA Kits) in lung epithelium enhances epithelial apoptosis and clearance of P. aeruginosa. Glutaredoxin-1 impairs bacterial clearance and increases severity of pneumonia in association with deglutathionylation of Fas (show FAS ELISA Kits).
GRX1 overexpression constrains oxidative stress and apoptosis in osteoarthritis chondrocytes by regulating CREB (show CREB1 ELISA Kits)/HO-1 (show HMOX1 ELISA Kits), providing a novel insight into the molecular mechanism and potential treatment of osteoarthritis.
Glutaredoxin 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 ELISA Kits) and Grx1 and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Prx2 (show PRDX2 ELISA Kits) glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 provide an alternative mechanism to thioredoxin (show TXN ELISA Kits) and thioredoxin reductase (show PRDX5 ELISA Kits) for Prx2 (show PRDX2 ELISA Kits) recycling.
Glutaredoxin 1 protects human retinal pigment epithelial cells from oxidative damage by preventing AKT (show AKT1 ELISA Kits) glutathionylation.
A new function for GRX1 in neuronal copper homeostasis and in protection from copper-mediated oxidative injury.
Human Grx1 can catalyse reduction of Atox1 (show ATOX1 ELISA Kits) by glutathione but only in the presence of Cu(I).
Levels of GLRX in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease.
Results indicate that the activation of eNOS (show NOS3 ELISA Kits)/NO system is regulated by Grx 1 and coupled with inhibition of JNK (show MAPK8 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) signaling pathway which could alleviate the oxidative stress/apoptosis in coronary arteries endothelial cells induced by HG.
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 (thioltransferase) pseudogene 3
, glutaredoxin (thioltransferase)-like
, glutaredoxin (grx-1)
, glutaredoxin Grx1
, glutaredoxin-1 (Grx1)
, thiol disulfide oxidoreductase
, glutaredoxin 1 (thioltransferase)