RRP8 antibody

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Description
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 sense the energy status of cell: upon glucose starvation, 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.
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Product specifications
Category | Primary Antibodies |
Immunogen Target | ribosomal RNA processing 8, methyltransferase, homolog(yeast) (RRP8) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | WB: 1:500-1:2000; IHC: 1:20-1:200; IF: 1:20-1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 51 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IF, IHC |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
UniProt ID | O43159 |
Gene ID | 23378 |
Alias | Ribosomal RNA-processing protein 8,Cerebral protein 1,Nucleomethylin,RRP8,KIAA0409,NML |
Background | Antibody anti-RRP8 |
Status | RUO |
Note | Mol. Weight 51 kDa |
Descripción
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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. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, 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.
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