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Human Glutaredoxin 1 Protein expressed in Escherichia coli (E. coli) - ABIN2181166
Yang, Jao, Nanduri, Starke, Mieyal, Qin: Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. in Biochemistry 1999
Show all 2 Pubmed References
Data suggest an essential role of hepatic Glrx in regulating SirT1 (zeige SIRT1 Proteine), which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.
Grx1 deficiency leads to eNOS (zeige NOS3 Proteine) dysfunction through oxidative modification of S-glutathionylation of eNOS (eNOS (zeige NOS3 Proteine)-SSG) and inactivation of NO production, enhancing the endothelial TLR4 (zeige TLR4 Proteine) 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 (zeige INS Proteine) secretion, increase of reactive oxygen species (ROS (zeige ROS1 Proteine)) 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 (zeige HIF1A Proteine) by increasing GSH adducts on Cys (zeige DNAJC5 Proteine)(520) promoting in vivo HIF-1alpha (zeige HIF1A Proteine) stabilization, VEGF-A (zeige VEGFA Proteine) production, and revascularization in the ischemic muscles.
Prx2 (zeige PRRX2 Proteine) 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 (zeige TXN Proteine) and thioredoxin reductase (zeige PRDX2 Proteine) for Prx2 (zeige PRRX2 Proteine) 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 (zeige IL17A Proteine)
Up-regulated Glrx inhibits VEGF signaling by increa (zeige FLT1 Proteine)sed Flt1 causing impaired vascularization.
Glutaredoxin-1 silencing induces cell senescence via p53/p21/p16 signaling axis.
Overexpression of NOS3 (zeige NANOS3 Proteine) increased the levels and activities of proteins of the redoxin systems, Trx1 (zeige MLL Proteine), Grx1, TrxR1 (zeige TXNRD1 Proteine) and TxnIP (zeige TXNIP Proteine), and the levels of signaling proteins (Akt1 (zeige AKT1 Proteine), pAkt1(-)Ser473, MapK (zeige MAPK1 Proteine), pMapK, Stat3 (zeige STAT3 Proteine), Fas (zeige FAS Proteine)).
Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes
GRX1 overexpression constrains oxidative stress and apoptosis in osteoarthritis chondrocytes by regulating CREB (zeige CREB1 Proteine)/HO-1 (zeige HMOX1 Proteine), 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 (zeige MLL Proteine) and Grx1 and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Prx2 (zeige PRDX2 Proteine) 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 (zeige TXN Proteine) and thioredoxin reductase (zeige PRDX5 Proteine) for Prx2 (zeige PRDX2 Proteine) recycling.
Glutaredoxin 1 protects human retinal pigment epithelial cells from oxidative damage by preventing AKT (zeige AKT1 Proteine) glutathionylation.
Results indicate that the activation of eNOS (zeige NOS3 Proteine)/NO system is regulated by Grx 1 and coupled with inhibition of JNK (zeige MAPK8 Proteine) and NF-kappaB (zeige NFKB1 Proteine) 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 1 (thioltransferase)
, glutaredoxin Grx1
, glutaredoxin (grx-1)
, glutaredoxin (thioltransferase)
, hypothetical protein
, thiol disulfide oxidoreductase
, glutaredoxin-1 (Grx1)
, glutaredoxin L homeolog