Rabbit anti-RRP8 Antibody Affinity Purified
Product Details
Specifications
The epitope recognized by A304-202A-T maps to a region between residue 406 to 456 of human Ribosomal RNA Processing 8 using the numbering given in entry NP_056139.1 (GeneID 23378).
Immunoglobulin concentration was determined using Beer’s Law where 1mg/mL IgG has an A280 of 1.4. Antibody was affinity purified using an epitope specific to RRP8 immobilized on solid support.
The epitope recognized by A304-202A maps to a region between residue 406 to 456 of human Ribosomal RNA Processing 8 using the numbering given in entry NP_056139.1 (GeneID 23378).
Immunoglobulin concentration was determined using Beer’s Law where 1mg/mL IgG has an A280 of 1.4.
Additional Product Information
Ribosomal RNA-processing protein (RRP8) is an 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 [taken from the Universal Protein Resource (UniProt) www.uniprot.org/uniprot/O43159].
Alternate Names
cerebral protein 1; KIAA0409; NML; nucleomethylin; ribosomal RNA processing 8, methyltransferase, homolog; ribosomal RNA-processing protein 8; RRP8 methyltransferase homolog
Applications
All western blot analysis is performed using 5% Milk-TBST for blocking and as antibody diluent. Primary antibody is incubated overnight.
Western blots of immunoprecipitates are performed using Goat anti-Rabbit Light Chain HRP Conjugate (Cat. No. A120-113P) with 5% Normal Pig Serum (Cat. No. S100-020) added to the blocking buffer.