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RbAp48 antibody [11G10]

GTX70232
GeneTex
ApplicationsFunctional Assay, ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin, Neutralisation/Blocking
Product group Antibodies
ReactivityHuman, Mouse
TargetRBBP4
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Overview

  • Supplier
    GeneTex
  • Product Name
    RbAp48 antibody [11G10]
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:500-1:3000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    Functional Assay, ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin, Neutralisation/Blocking
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    11G10
  • Concentration
    1 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID5928
  • Target name
    RBBP4
  • Target description
    RB binding protein 4, chromatin remodeling factor
  • Target synonyms
    NURF55, RBAP48, lin-53, histone-binding protein RBBP4, CAF-1 subunit C, CAF-I 48 kDa subunit, CAF-I p48, MSI1 protein homolog, RBBP-4, chromatin assembly factor 1 subunit C, chromatin assembly factor I p48 subunit, chromatin assembly factor/CAF-1 p48 subunit, nucleosome-remodeling factor subunit RBAP48, retinoblastoma-binding protein 4, retinoblastoma-binding protein p48
  • Host
    Mouse
  • Isotype
    IgG2b
  • Protein IDQ09028
  • Protein Name
    Histone-binding protein RBBP4
  • Scientific Description
    This gene encodes a ubiquitously expressed nuclear protein which belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2 complex which has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of co-repressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008]
  • Reactivity
    Human, Mouse
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Soontornniyomkij V, Chang RC, Soontornniyomkij B, et al. Loss of Immunohistochemical Reactivity in Association With Handling-Induced Dark Neurons in Mouse Brains. Toxicol Pathol. 2020,48(3):437-445. doi: 10.1177/0192623319896263
    Read this paper
  • Kosmidis S, Polyzos A, Harvey L, et al. RbAp48 Protein Is a Critical Component of GPR158/OCN Signaling and Ameliorates Age-Related Memory Loss. Cell Rep. 2018,25(4):959-973.e6. doi: 10.1016/j.celrep.2018.09.077
    Read this paper
  • Chou HC, Lu CH, Su YC, et al. Proteomic analysis of honokiol-induced cytotoxicity in thyroid cancer cells. Life Sci. 2018,207:184-204. doi: 10.1016/j.lfs.2018.06.002
    Read this paper
  • Chang LC, Lin HY, Tsai MT, et al. YC-1 inhibits proliferation of breast cancer cells by down-regulating EZH2 expression via activation of c-Cbl and ERK. Br J Pharmacol. 2014,171(17):4010-25. doi: 10.1111/bph.12708
    Read this paper
  • Pavlopoulos E, Jones S, Kosmidis S, et al. Molecular mechanism for age-related memory loss: the histone-binding protein RbAp48. Sci Transl Med. 2013,5(200):200ra115. doi: 10.1126/scitranslmed.3006373
    Read this paper
  • Chen PL, Chen CF, Chen Y, et al. Mitochondrial genome instability resulting from SUV3 haploinsufficiency leads to tumorigenesis and shortened lifespan. Oncogene. 2013,32(9):1193-201. doi: 10.1038/onc.2012.120
    Read this paper
  • Hirose N, Maekawa T, Shinagawa T, et al. ATF-2 regulates lipopolysaccharide-induced transcription in macrophage cells. Biochem Biophys Res Commun. 2009,385(1):72-7. doi: 10.1016/j.bbrc.2009.05.001
    Read this paper
  • Yamagoe S, Kanno T, Kanno Y, et al. Interaction of histone acetylases and deacetylases in vivo. Mol Cell Biol. 2003,23(3):1025-33.
    Read this paper
  • Zegerman P, Canas B, Pappin D, et al. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem. 2002,277(14):11621-4.
    Read this paper
  • Nicolas E, Ait-Si-Ali S, Trouche D. The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein. Nucleic Acids Res. 2001,29(15):3131-6.
    Read this paper