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Redox sensor protein. Zusätzlich bieten wir Ihnen NMRAL1 Antikörper (20) und NMRAL1 Kits (8) und viele weitere Produktgruppen zu diesem Protein an.
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These findings suggest that the increased susceptibility of the G6PD (zeige G6PD Proteine)-knockdown cells to viral infection was due to impaired NF-kappaB (zeige NFKB1 Proteine) signaling and antiviral response mediated by HSCARG.
After viral infection, HSCARG interacted with tumor necrosis receptor-associated factor 3 (TRAF3 (zeige TRAF3 Proteine)) and inhibited its ubiquitination by promoting the recruitment of OTUB1 (zeige OTUB1 Proteine) to TRAF3 (zeige TRAF3 Proteine).
Data indicate that HSCARG and USP7 (zeige USP7 Proteine) function in concert in inhibiting polyubiquination of NEMO (zeige IKBKG Proteine), thus inhibiting NF-kappaB (zeige NFKB1 Proteine) activity.
HSCARG is involved in DNA damage response through affecting the level of H2A ubiquitination and localization of RAP80 (zeige UIMC1 Proteine) at lesion points.
HSCARG regulated reactive-oxygen-species homeostasis through inhibition of NADPH oxidase activity via regulation of the expression of p47phox.
CRM1 (zeige XPO1 Proteine) dependent nucleocytoplasmic translocation of HSCARG plays an important role in fine-tuning NF-kappaB (zeige NFKB1 Proteine) signaling
HSCARG is involved in the NF-kappaB (zeige NFKB1 Proteine) signaling pathway, and negatively regulates NF-kappaB (zeige NFKB1 Proteine) activation.
expression, crystallization and preliminary X-ray crystallographic studies of HSCARG at a resolution of 2.4 A; crystals belong to F23 (zeige CISH Proteine) space group, with unit cell parameters a=b=c=223.30A, alpha=beta=gamma=90 degrees
One of the functions regulated by HSCARG may be argininosuccinate synthetase that is involved in NO synthesis
HSCARG regulation of argininosuccinate synthetase activity is crucial for maintaining the intracellular balance between redox state and nitric oxide levels
Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity).
nmrA-like family domain-containing protein 1
, short chain dehydrogenase/reductase family 48A, member 1