产品描述： background: In the nucleus, DNA is tightly packed into nucleosomes generating an environment which is highly repressive towards DNA

processes such as transcription. Acetylation of lysine residues within proteins has emerged as an important mechanism used

by cells to overcome this repression. The acetylation of non-histone proteins such as transcription factors, as well as histones

appears to be involved in this process. Acetylation may result in structural transitions as well as specific signaling within discrete

chromatin domains. The role of acetylation in intracellular signaling has been inferred from the binding of acetylated peptides by

the conserved bromodomain. Furthermore, recent findings suggest that bromodomain/acetylated-lysine recognition can serve as

a regulatory mechanism in protein-protein interactions in numerous cellular processes such as chromatin remodeling and

transcriptional activation. The reversible lysine acetylation of histones and non-histone proteins plays a vital role in the regulation

of many cellular processes including chromatin dynamics and transcription, gene silencing, cell cycle progression, apoptosis,

differentiation, DNA replication, DNA repair, nuclear import, and neuronal repression. More than 20 acetyltransferases and 18

deacetylases have been identified so far, but the mechanistic details of substrate selection and site specificity of these enzymes

remain unclear. Over 40 transcription factors and 30 other nuclear, cytoplasmic, bacterial, and viral proteins have been shown to be

acetylated in vivo.