Anti-Histone H2AXK5Ac Rabbit (Clone RM445)

Histone H2AX is a variant of histone H2A, a nuclear protein and a component of the nucleosome core. 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. H2AX has a key role in the DNA damage response. Ionizing radiation induces acetylation of lysine 5 on H2AX (H2AXK5Ac) by TIP60, which is recognized by a bromodomain-like module in DNA protein kinase (DNA-PK). DNA-PK and other PI3K-like kinases ataxia-telangiectasia mutated kinase (ATM) and ataxia-telangiectasia and Rad3-related protein/kinase (ATR) phosphorylate serine 139 on H2AX (gammaH2AX) 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. Decreased tumor H2AX levels are associated with increased progression-free survival in patients with triple-negative breast cancer. Cayman's Histone H2AXK5Ac Rabbit Monoclonal Antibody (Clone RM445) can be used for multiplex-based assay and Western blot (WB) applications. The antibody recognizes H2AXK5Ac at 15 kDa from human and other vertebrate samples.. Cross reactivity: (+) H2AXK5Ac: (-) H2AXK9Ac, (-) H2AXK36Ac, (-) H2AZK4Ac, (-) H2AZK7Ac, (-) H2AZK11Ac, (-) H2AZK13Ac, (-) Unmodified H2AXK5, (-) Unmodified H2AXN19, (-) Unmodified H2AXK36. (+) Human: (+) Vertebrates.. Protein function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post- translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation. [The UniProt Consortium]