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The protein encoded by RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. De plus, nous expédions RNF40 Anticorps (59) et et beaucoup plus de produits pour cette protéine.
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Our results support a model in which the direct function of RNF40-mediated H2B monoubiquitination increases transcriptional elongation by promoting the spreading of H3K4me3 into the 5' transcribed region of a select subgroup of genes.
We show that Bre1 (Montrer RNF20 Protéines) (human BRE1A (Montrer RNF20 Protéines)/B (RNF20 (Montrer RNF20 Protéines)/40) and mouse Bre1a (Montrer RNF20 Protéines)/b (Rnf20 (Montrer RNF20 Protéines)/40)) acts as an important suppressor of chromosomal instability
the observed defects in the radiation response of Bre1a (Montrer RNF20 Protéines)/b-deficient cells
the RNF20 (Montrer RNF20 Protéines)/40 complex, a major ubiquitin ligase catalysing histone H2B monoubiquitination, interacts with the motor protein Eg5 (Montrer KIF11 Protéines) during mitosis and participates in spindle assembly.
The authors also show that the RING domains of RNF20 (Montrer RNF20 Protéines) and RNF40 can form a stable heterodimer that is active.
Manipulation of key H2Bub1 E3 ubiquitin ligases, RNF20 (Montrer RNF20 Protéines), RNF40 and BRCA1, in ovarian cancer cell line models modulated H2Bub1 levels, indicative of the role of these RING finger (Montrer PCGF1 Protéines) ligases in monoubiquitination of H2Bub1 in vitro
our results suggest that RNF20 and RNF40, either via ubiquitylation of H2B or other targets, are coupled to the proliferation of prostate cancer cells.
RNF40 cooperates with SUPT16H (Montrer SUPT16H Protéines) to induce dynamic changes in chromatin structure during DNA double-strand break repair.
Studies indicate that H2B monoubiquitylation is driven primarily by an E3 ubiquitin ligase (Montrer MUL1 Protéines) composed of the two RING finger (Montrer PCGF1 Protéines) proteins RNF20 (Montrer RNF20 Protéines) and RNF40.
Formation of trimeric complex UbcH6 and RNF20/40 with PAF stimulates histone 2B monoubiquitination activity in vitro
The protein encoded by this gene contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the rat counterpart suggested that this protein may function as an E3 ubiquitin-protein ligase, and facilitate the ubiquitination and degradation of syntaxin 1, which is an essential component of the neurotransmitter release machinery. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, E3 ubiquitin-protein ligase BRE1B
, 95 kDa retinoblastoma protein binding protein
, 95 kDa retinoblastoma-associated protein
, BRE1 E3 ubiquitin ligase homolog B
, Rb-associated protein
, protein staring
, staring protein
, syntaxin-1-interacting RING finger protein