Date published: 2025-10-18

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p-Histone H2A.X Antibody (Ser 139): sc-517348

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Datasheets
  • p-Histone H2A.X Antibody (Ser 139) is a mouse monoclonal IgG1, cited in 116 publications, provided at 50 µg/0.5 ml
  • raised against a recombinant protein corresponding to the Ser 139 phosphorylated region of Histone H2A.X of human origin
  • recommended for detection of Ser 139 phosphorylated Histone H2A.X of mouse, rat and human origin by WB, IP and IF
  • At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for p-Histone H2A.X Antibody (Ser 139). This work is in progress.

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p-Histone H2A.X Antibody (Ser 139) is a mouse monoclonal IgG1 antibody that detects Ser 139 phosphorylated Histone H2A.X (p-H2A.X) in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). anti-p-H2A.X antibody (Ser 139) is available in a non-conjugated form, allowing for versatile experimental setups. Histone H2A.X plays a crucial role in cellular response to DNA damage, particularly in recognizing and repairing double-stranded breaks. Upon DNA damage, H2A.X is rapidly phosphorylated at Ser 139, forming γ-H2A.X, which serves as a marker for DNA damage and is essential for recruiting repair proteins to injury sites. This phosphorylation event is critical for nuclear foci formation, where repair factors such as Rad50, Rad51, and BRCA1 are recruited to facilitate repair. γ-H2A.X not only indicates DNA damage but also plays a pivotal role in signaling pathways that activate cellular repair mechanisms, making γ-H2A.X an important target for studies related to genomic stability and cancer research.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.

Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA

LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences

p-Histone H2A.X Antibody (Ser 139) References:

  1. Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139.  |  Rogakou, EP., et al. 2000. J Biol Chem. 275: 9390-5. PMID: 10734083
  2. A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage.  |  Paull, TT., et al. Curr Biol. 10: 886-95. PMID: 10959836
  3. Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress.  |  Ward, IM. and Chen, J. 2001. J Biol Chem. 276: 47759-62. PMID: 11673449
  4. AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching.  |  Petersen, S., et al. 2001. Nature. 414: 660-665. PMID: 11740565
  5. Histone phosphorylation: a chromatin modification involved in diverse nuclear events.  |  Rossetto, D., et al. 2012. Epigenetics. 7: 1098-108. PMID: 22948226
  6. Phosphorylated histone H2A.x in porcine embryos produced by IVF and somatic cell nuclear transfer.  |  Bohrer, RC., et al. 2013. Reproduction. 146: 325-33. PMID: 23858475
  7. Resveratrol induces H3 and H4K16 deacetylation and H2A.X phosphorylation in Toxoplasma gondii.  |  Contreras, SM., et al. 2021. BMC Res Notes. 14: 19. PMID: 33413578
  8. Exposure to fluoride exacerbates the cognitive deficit of diabetic patients living in areas with endemic fluorosis, as well as of rats with type 2 diabetes induced by streptozotocin via a mechanism that may involve excessive activation of the poly(ADP ribose) polymerase-1/P53 pathway.  |  Xiang, J., et al. 2024. Sci Total Environ. 912: 169512. PMID: 38145685
  9. Structure of the mouse H2A.X gene and physical linkage to the UPS locus on chromosome 9: assignment of the human H2A.X gene to 11q23 by sequence analysis.  |  Porcher, C. and Grandchamp, B. 1995. Genomics. 25: 312-3. PMID: 7774939
  10. Characterization of the human histone H2A.X gene. Comparison of its promoter with other H2A gene promoters.  |  Ivanova, VS., et al. 1994. J Biol Chem. 269: 24189-94. PMID: 7929075

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

p-Histone H2A.X Antibody (Ser 139)

sc-517348
50 µg/0.5 ml
$316.00