Render Target: STATIC
Render Timestamp: 2024-11-28T12:49:19.625Z
Commit: d79925545b26f8827f92d145dadc6f0527debdb1
XML generation date: 2024-08-01 15:24:21.492
Product last modified at: 2024-10-17T11:45:30.966Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464
  1. Products /
  2. Primary Antibodies /
  3. Nucleomethylin Antibody

Nucleomethylin Antibody #4789

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 58
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    This antibody detects endogenous levels of total Nucleomethylin protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of the human Nucleomethylin protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Nucleomethylin (NML), also known as ribosomal RNA-processing protein 8 (RRP8) and human cerebral protein 1 (Hucep-1), is a nucleolar protein (1,2). NML interacts with the histone de-acetylase protein SirT1 and histone methyl-transferase protein SUV39H1 to form the energy-dependent nucleolar silencing complex (eNoSC) that regulates ribosomal RNA (rRNA) transcription in response to changes in the energy state of the cell (2). As energy levels in the cell decrease due to caloric restriction, eNoSC binds to rRNA genes and represses transcription by SirT1-mediated de-acetylation of histones and SUV39H1-mediated methylation of histone H3 on Lys9. NML binds to di-methylated Lys9 of histone H3 and likely functions in the recruitment and spreading of eNoSC along the rRNA genes (2). NML also contains a methyltransferases-like domain, which binds to S-adenosyl-methionine (SAM) and is required for eNoSC function (2). By limiting the transcription of rRNA genes during caloric restriction, eNoSC promotes the restoration of energy balance and protects cells from energy-dependent apoptosis.

    Database Links

    UniProt ID: O43159


    Entrez-Gene Id: 23378


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    For Research Use Only. Not For Use In Diagnostic Procedures.
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