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Human Polyclonal RNF4 Primary Antibody für WB - ABIN1537658
Wang, Sang, Ren, Liu, Liu, Zhang, Wang, Wang, Orian, Yang, Yi: SENP3 regulates the global protein turnover and the Sp1 level via antagonizing SUMO2/3-targeted ubiquitination and degradation. in Protein & cell 2015
Respiratory syncytial virus induces NRF2 (zeige GABPA Antikörper) degradation through a PML (zeige PML Antikörper)-RNF4 pathway.
Thus, although Rnf4 and Ube2w (zeige UBE2W Antikörper) functionally interact in vitro, these genetic experiments indicate that in response to DNA damage Ube2w (zeige UBE2W Antikörper) and Rnf4 function in distinct pathways.
The E3 ligase RNF4 is required to ubiquitinate FXR (zeige NR1H4 Antikörper) in response to SUMOylation.
RNF4-dependent ubiquitylation translates transient phosphorylation signal(s) into long-term protein stabilization, resulting in enhanced oncoprotein activation
These findings indicate that SUMOylation of NDRG2 (zeige NDRG2 Antikörper) is necessary for its tumor suppressor function in lung adenocarcinoma and that RNF4 increases the efficiency of this process.
post-translational modification of Nkx3.2 (zeige NKX3-2 Antikörper) employing HDAC9 (zeige HDAC9 Antikörper)-PIASy (zeige PIAS4 Antikörper)-RNF4 axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates.
These findings illustrate a novel strategy for viral interference with the SUMO pathway, and identify the EBV miR (zeige MLXIP Antikörper)-BHRF1-1 and the cellular RNF4 as regulators of the productive virus cycle.
These results point to an important role of the affinity between RNF4 and its cognate RAD6B (zeige UBE2B Antikörper) or UBCH5B (zeige UBE2D2 Antikörper) in governing the multiplicity of substrate ubiquitination.
the opposing activities of RNF4 and ataxin-3 (zeige ATXN3 Antikörper) consolidate robust MDC1 (zeige MDC1 Antikörper)-dependent signaling and repair ofDNA double-strand break.
Combined effect of dynamic recruitment of RNF4 to KAP1 regulates the relative occupancy of 53BP1 and BRCA1 at double-strand break sites to direct DNA repair in a cell cycle-dependent manner.
These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure.
This paper identifies a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones.
fork collapse in Atr (zeige ATR Antikörper)-deleted cells is mediated through the combined effects the sumo targeted E3-ubiquitin ligase RNF4 and activation of the AURKA (zeige AURKA Antikörper)-PLK1 (zeige PLK1 Antikörper) pathway
Rnf4 controls protein localization at DNA damage sites by integrating SUMOylation and ubiquitylation events.
SUMO interacting motif is dispensable for PML (zeige PML Antikörper) SUMOylation and interaction with RNF4 but is required for efficient PML (zeige PML Antikörper) ubiquitination, recruitment of proteasome components within NBs (zeige NLRP2 Antikörper) and proteasome-dependent degradation of PML (zeige PML Antikörper) in response to AsO
Rnf4 deficiency is embryonic lethal with higher levels of methylation in genomic DNA. Mechanistic studies show that RNF4 interacts with and requires the base excision repair enzymes TDG (zeige TDG Antikörper) and APE1 (zeige APEX1 Antikörper) for active demethylation.
GC-rich (zeige RELB Antikörper) elements flanking the transcription start site govern activation
1.6- and 3.0-kb transcripts originate from the same promoter, encode for the same protein and differ in the 3' UTR (zeige UTS2R Antikörper).
RNF4 is a negative regulator of TRPS1 (zeige TRPS1 Antikörper) activity
results suggest a role for small nuclear ring finger protein(SNURF/RNF4) in fetal germ cell development as well as in oocyte and granulosa cell maturation in an estrogen- and gonadotropin-regulated fashion
The protein encoded by this gene contains a RING finger motif and acts as a transcription regulator. This protein has been shown to interact with, and inhibit the activity of, TRPS1, a transcription suppressor of GATA-mediated transcription. Transcription repressor ZNF278/PATZ is found to interact with this protein, and thus reduce the enhancement of androgen receptor-dependent transcription mediated by this protein. Studies of the mouse and rat counterparts suggested a role of this protein in spermatogenesis. A pseudogene of this gene is found on chromosome 1.
E3 ubiquitin ligase RNF4
, E3 ubiquitin-protein ligase RNF4
, small nuclear RING finger protein
, gene trap ROSA b-geo 8
, small nuclear ring finger protein
, RING finger protein 4