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Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. Additionally we are shipping RRP8 Antibodies (22) and many more products for this protein.
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NML depletion increases 60S ribosomal protein L11 (RPL11 (show RPL11 Proteins)) levels in the ribosome-free fraction and protein levels of p53 (show TP53 Proteins) through an RPL11 (show RPL11 Proteins)-MDM2 (show MDM2 Proteins) complex, which activates the p53 (show TP53 Proteins) pathway.
Among Systemic lupus erythematosus patients, 63.6% and 45.5% of those with lupus nephritis were positive for anti-RRP8 and anti-TNP1 (show TNP1 Proteins) antibodies, compared with 12.5% and 9.4% of Systemic lupus erythematosus patients without nephritis, respectively.
Data indicate that the the nucleomethylin (NML)-SirT1 (show SIRT1 Proteins) interaction was competitively inhibited by rRNA.
Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys- 9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown.
RRP8 methyltransferase homolog
, cerebral protein 1
, ribosomal RNA-processing protein 8
, cerebral protein 1 homolog