Product Datasheet  
Histone H2A.X(Phospho-Ser139) Antibody  
Catalog Number: 11268  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot: P16104
    NCBI Protein: NP_002096.1
  • Form of Antibody：  
  • Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage：  
  • Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
  • Immunogen：  
  • Peptide sequence around phosphorylation site of serine 139 (Q-A-S(p)-Q-E) derived from Human Histone H2A.X.
  • reactivity：  
  • Hu
  • appl_detail：  

  • Predicted MW: 15kd
    Western blotting: 1:500~1:1000
    Immunofluorescence: 1:100~1:200

  • other_names：  
  • H2A.X; H2AFX; H2a/x; HIST5-2AX;
  • Purification：  
  • Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
  • Specificity：  
  • The antibody detects endogenous level of Histone H2A.X only when phosphorylated at serine 139.
  • Applications：  
  • WB IF
  • Background：  

  • Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.

    Yaneva M, et al. (2005) Nucleic Acids Res. 33(16): 5320-5330.
    Tsukuda T, et al.(2006) Nature. Author manuscript; available in PMC 2006 March 6.




 
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