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RNF125 encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. Zusätzlich bieten wir Ihnen RNF125 Antikörper (62) und und viele weitere Produktgruppen zu diesem Protein an.
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study identifies new gene-type zinc finger protein 125 (RNF125) as a negative regulator of TRIM14 in the innate antiviral immune response
Data indicate that brain from Japanese encephalitis virus (JEV)-infection showed a reciprocal correlation between microRNA miR-15b levels and the expression of ring finger protein 125 (RNF125).
RNF125 is enhanced by IFN, these functions constitute a negative regulatory loop circuit for IFN production
this study shows that RNF125 activates Interleukin-36 receptor signaling and contributes to its turnover
for the ubiquitin ligase RNF125 that, in addition to the RING domain, a C2HC Zn finger (ZnF) is crucial for activity.
high RNF125 expression is related with aggressive characteristics and unfavorable prognosis of GBC patients; RNF125 promotes the invasion and metastasis of human GBCs via activating the TGF-beta1-SMAD3-ID1 signaling pathway.
we identified the downregulation of the ubiquitin ligase RNF125 in BRAFi-resistant melanomas
Results indicate that the nucleotide sequence in the 3' untranslated region (3' UTR) of ring finger protein 125 (RNF125) is a potential microRNA miR-15b targeting site.
studies of the RNF125 pathway point to upregulation of RIG-I-IPS1-MDA5 and/or disruption of the PI3K-AKT and interferon signaling pathways as the putative final effectors
In controls, RNF125 is the highest expressed gene, whereas in HIV infection progressors, RIG-I is either the highest expressed gene or is expressed similarly to RNF125 and TRIM25.
study reports human bocavirus VP2 modulates IFN pathway by targeting the ring finger protein 125, a negative regulator of type I IFN signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I and leads to the proteasome-dependent degradation of RIG-I
These results suggest that RNF125/TRAC-1 could function to recruit host factor(s) controlling HIV-1 transcription to the ubiquitin-proteasome pathway.
TRAC-1 associates with membranes and is excluded from the nucleus through myristoylation
This gene encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. As a result of myristoylation, this protein associates with membranes and is primarily localized to intracellular membrane systems. The encoded protein may function as a positive regulator in the T-cell receptor signaling pathway.
E3 ubiquitin-protein ligase RNF125
, T-cell RING activation protein 1
, T-cell ring protein identified in activation screen