The Bromodomain Ligand 2 is peptide histone H3 (1-21), acetylated at lysine 14. It contains a C-terminal GG linker, followed by a biotinylated Lys. Bromodomains function as acetyl-lysine binding domains, and bromodomain/acetyl-lysine recognition can regulate histone modification, DNA replications, chromatin remodeling, and gene transcription. This peptide is suitable for use as a ligand for several bromodomains including ATAD2 and BAZ2B.
The pattern of histone H4 acetylation in different genomic regions has been investigated by immunoprecipitating oligonucleosomes from a human lymphoblastoid cell line with antibodies to H4 acetylated at lysines 5, 8, 12 or 16. DNA from antibody-bound or unbound chromatin
Reversible acetylation of nucleosomal histones H3 and H4 generally is believed to be correlated with potential transcriptional activity of eukaryotic chromatin domains. Here, we report that the extent of H4 acetylation within euchromatin and heterochromatic domains is linked with DNA
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