Anti-H2AX pS139 antibodies, human and mouse

Anti-H2AX pS139 antibodies, human and mouse

Clone: REA502 | Dilution: 1:11
Clone REA502 recognizes the human and mouse histone H2AX antigen phosphorylated at serine 139 (pS139). H2AX is a 14 kDa basal histone and a variant of the H2 histone family. It replaces conventional H2A in a subset of nucleosomes. When cells are exposed to ionizing radiation or DNA-damaging chemotherapeutic agents, double-stranded breaks (DSBs) are generated that rapidly result in the phosphorylation of H2AX at serine 139 (γH2AX). Because phosphorylation of H2AX is abundant, fast, and correlates well with each DSB, it is the most sensitive marker that can be used to examine the DNA damage produced and the subsequent repair of the DNA lesion. γH2AX also participates in the evolutionarily conserved process of sister chromatid recombination, a homologous recombination pathway involved in the suppression of genomic instability during DNA replication and directly implicated in tumor suppression.
Additional information: Clone REA502 displays negligible binding to Fc receptors.

Alternative names

H2AFX, H2AX, H2a/x, H2A.X, γ-H2AX, γH2AX

Technical specifications

  • Antigen: H2AX pS139
  • Clone: REA502
  • Isotype: recombinant human IgG1
  • Isotype control: REA Control (I) antibodies
  • Alternative names of antigen: H2AFX, H2AX, H2a/x, H2A.X, γ-H2AX, γH2AX
  • Entrez Gene ID: 3014, 15270
  • Molecular mass of antigen [kDa]: 15
  • Distribution of antigen: ubiquitous
  • Product format: Reagents are supplied in buffer containing stabilizer and 0.05% sodium azide.
  • Fixation: The antibody is suited for staining of formaldehyde-fixed cells.
  • Storage: Store protected from light at 2–8 °C. Do not freeze.
  • Available conjugates: PE, APC
  • Selected references

    1. Mannironi, C. et al. (1989) H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals. Nucleic Acids Res. 17(22): 9113-9126
    2. Paull, T. T. et al. (2000) A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr. Biol. 10(15): 886-895
    3. Sharma, A. et al. (2012) Histone H2AX phosphorylation: a marker for DNA damage. Methods Mol. Biol. 920: 613-626
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