Anti-phospho-Histone H2AvD (Ser137)

This affinity purified anti-Histone H2AvD pS137 Antibody is directed against the phosphorylated form of Drosophila H2AvD protein at the pS137 residue. The product was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross-adsorbed against the non-phosphorylated form of the immunizing peptide. Reactivity occurs against Drosophila H2AvD pS137 protein and the antibody is specific for the phosphorylated form of the protein. Reactivity with non-phosphorylated Drosophila H2AvD is minimal by ELISA. A BLAST analysis was used to suggest little to no cross reactivity with H2AvD proteins from other sources based on a comparison using the immunizing sequence. Reactivity against homologues from other sources is not known. 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. Acts as a Polycomb group (PcG) protein required to maintain the transcriptionally repressive state of homeotic genes of the animal throughout development. Required for histone H3 'Lys-9' methylation and histone H4 'Lys-12' acetylation, two modifications that are essential for heterochromatin formation. Also involved in DNA double strand break (DSB) repair. Essential for early development. [The UniProt Consortium]