A synthetic phospho-peptide corresponding to residues surrounding serine 28 and serine 31 of human Histone H3.3 protein.
Buffer
Store at -20C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Various post-translational modifications, such as acetylation and methylation, of core histones serve as regulators of gene expression (2). Histone H3.3 is a variant histone which replaces conventional H3 in nucleosomes in active genes. It is predominant from of histone H3 in non-dividing cells and it is incorporated into chromatin independently of DNA synthesis. H3.3 is phosphorylated at serine 28 by MLTK isoform 1, RPS6KA5, and AURKB during mitosis. Also, phosphorylation at serine 31 on H3.3 is specific to regions bordering centromeres in metaphase chromosomes.
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