Anti-Histone H2A (yeast) (phospho S129) antibody (ab17353)

Overview

  • Product nameAnti-Histone H2A (yeast) (phospho S129) antibody
    See all Histone H2A primary antibodies
  • Description
    Rabbit polyclonal to Histone H2A (phospho S129)
  • Tested applicationsSuitable for: WBmore details
  • Species reactivity
    Reacts with: Schizosaccharomyces pombe
    Predicted to work with: Saccharomyces cerevisiae
  • Immunogen

    Synthetic peptide corresponding to Schizosaccharomyces pombe Histone H2A aa 100 to the C-terminus (C terminal) (phospho S129) conjugated to Keyhole Limpet Haemocyanin (KLH).
    Database link: P04910
    (Peptide available as ab17576)

  • Positive control
    • S. pombe lysate

Properties

  • FormLiquid
  • Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
  • Storage bufferPreservative: 0.02% Sodium Azide
    Constituents: 1% BSA, PBS, pH 7.4
  • Concentration information loading...
  • PurityImmunogen affinity purified
  • ClonalityPolyclonal
  • IsotypeIgG
  • Research areas

Associated products

Applications

Our Abpromise guarantee covers the use of ab17353 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB Use a concentration of 1 µg/ml. Detects a band of approximately 15.5 kDa (predicted molecular weight: 15.5 kDa).

Target

  • RelevanceCore component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Post-translational modification for Saccharomyces cerevisiae: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. N-acetylated by NAT4. Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac. Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. Sumoylated to from H2AK126su. May lead to transcriptional repression. Post-translational modification for Schizosaccharomyces pombe: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. Acetylated by esa1 to form H2AK4ac and H2AK7ac.
  • Cellular localizationNuclear
  • Database links
    • Alternative names
      • H2A1 antibody
      • H2A2 antibody
      • Histone H2A-alpha antibody
      • Histone H2A-beta antibody
      • Histone H2A.1 antibody
      • Histone H2A.2 antibody
      • Hta 1 antibody
      • HTA 2 antibody
      • Hta1 antibody
      • Hta1p antibody
      • HTA2 antibody
      • Hta2p antibody
      • SPT 11 antibody
      • SPT11 antibody
      see all

    Anti-Histone H2A (yeast) (phospho S129) antibody images

    • All lanes : Anti-Histone H2A (yeast) (phospho S129) antibody (ab17353) at 1 µg/ml

      Lane 1 : S. pombe lysate (0.1 ug)
      Lane 2 : S. pombe lysate (0.1 ug) with S. pombe Histone H2A (phospho S129) peptide (ab17576) at 1 µg/ml
      Lane 3 : S. pombe lysate (0.1 ug) with S. pombe Histone H2A (unmodified ) peptide (ab17577) at 1 µg/ml


      Predicted band size : 15.5 kDa

    References for Anti-Histone H2A (yeast) (phospho S129) antibody (ab17353)

    This product has been referenced in:
    • Tapia-Alveal C  et al. H2A.Z-dependent regulation of cohesin dynamics on chromosome arms. Mol Cell Biol 34:2092-104 (2014). Read more (PubMed: 24687850) »
    • Outwin EA  et al. Smc5-Smc6-dependent removal of cohesin from mitotic chromosomes. Mol Cell Biol 29:4363-75 (2009). WB ; Schizosaccharomyces pombe . Read more (PubMed: 19528228) »

    See all 2 Publications for this product

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    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"