Histone H2AX (C-Term) Monoclonal Antibody (Clone RM214)

Histone H2AX is a variant of histone H2A, a nuclear protein and a component of the nucleosome core.^1,2 It is a globular protein containing unstructured N- and C-terminal tails that extend outside of the nucleosome core that are subject to a variety of post-translational modifications (PTMs), including phosphorylation, acetylation, methylation, and ubiquitination, which function as epigenetic regulators of transcription.^3,4 H2AX has a key role in the DNA damage response.^3,4,1,5 It is phosphorylated at serine 139 (γH2AX) by the PI3K-like kinases ATM, ATR, and DNA-PK in response to DNA damage, leading to changes in chromatin structure at the damaged site that promote DNA repair. H2AX has additional roles in chromatin inactivation during meiosis and mitosis, as well as neural stem cell development and cellular senescence.⁵ Decreased tumor H2AX levels are associated with increased progression-free survival in patients with triple-negative breast cancer.⁶ Cayman's Histone H2AX (C-Term) Monoclonal Antibody (Clone RM214) can be used for ELISA, immunocytochemistry (ICC), multiplex-based assay, and Western blot (WB) applications. The antibody recognizes the C-terminal region of histone H2AX independent of PTMs.

WARNING This product is not for human or veterinary use.

1. Bönisch, C., and Hake, S.B. Histone H2A variants in nucleosomes and chromatin: More or less stable? Nucleic Acids Res. 40(21), 10719-10741 (2012).

2. Hyun, K., Jeon, J., Park, K., et al. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).

3. Dickey, J.S., Redon, C.E., Nakamura, A.J., et al. H2AX: Functional roles and potential applications. Chromosoma 118(6), 683-692 (2009).

4. Corujo, D., and Buschbeck, M. Post-translational modifications of H2A histone variants and their role in cancer. Cancers (Basel) 10(3), 59 (2018).

5. Turinetto, V., and Giachino, C. Multiple facets of histone variant H2AX: A DNA double-strand-break marker with several biological functions. Nucleic Acids Res. 43(5), 2489-2498 (2015).

6. Gruosso, T., Mieulet, V., Cardon, M., et al. Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients. EMBO Mol. Med. 8(5), 527-549 (2016).