ɣH2AX (pS139) peptide
Antigenic peptide from histone variant H2AX, phosphorylated at serine 139
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 References
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
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.