ɣH2AX (pS139) peptide

  • Description

  • Application Data


Antigenic peptide from histone variant H2AX, phosphorylated at serine 139

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Application Data

Catalogue number crb1200386
Antibody ɣH2AX (pS139) peptide
Antigen Peptide ɣH2AX (pS139) peptide
Protein ID UniProtKB - P16104
Aliases Phosphorylated Histone H2AX (pS139)
Cross-Reactivity Human
Target Protein Species Human
Storage Stabilisers -20°C
Specificity Protein
Storage -20°C

Feng, Y., Xiang, J., Liu, S., Guo, T., Yan, G., Feng, Y., Kong, N., Li, H., Huang, Y., Lin, H., Cai, X. and Xie, A. (2017). H2AX facilitates classical non-homologous end joining at the expense of limited nucleotide loss at repair junctions. Nucleic Acids Res, 45(18), 10614-10633. PMID: 28977657


Kuo LJ1, Yang LX. (2008). Gamma-H2AX – a novel biomarker for DNA double-strand breaks. In Vivo, 22(3), 305-9. PMID: 18610740

Data Sheet Material Safety Data Sheet (MSDS)

Antigenic peptide from H2A histone variant H2AX with phosphorylated serine 139. H2AX is rapidly phosphorylated on serine 139 in response to DNA double strand breaks (DSBs). DSBs occur as part of the natural process of meiosis, and in response to external stimuli and mutagens. In either form, DSBs pose a huge threat to genome integrity and must be repaired quickly and accurately.

In mammalian cells, repair of DSBs is carried out primarily by either homologous recombination (HR) or non-homologous end joining (NHEJ). Upon DNA damage, phosphorylated H2AX, termed ‘γH2AX’, quickly accumulates and initiates a DNA damage signalling cascade at the DSB site. γH2AX also alters the chromatin at the DSB site to form an area accessible to the protein interactions and modifications required for DSB repair.

ɣH2AX (pS139) peptide

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