Histone acetylation is defined by the addition of an acetyl functional group to the lysine residues of the N-terminal tail and its status can be studied with the use of histone acetylation antibodies. Evidence shows histone acetylation is highly involved in gene regulation and histone acetyltransferase (HAT) and histone deacetylase (HDAC) activity affect the availability of chromatin to gene transcription.
The process of histone acetylation at lysine residues by histone acetyltransferase (HAT) is an important epigenetic marker and can be measured with the use of histone lysine acetylation antibodies. Acetylation of histones reduces the interaction of histone N termini with the phosphate groups of DNA, thereby loosening chromatin and opening it up for increased gene transcription. Acetylation of H3K14, for instance, has been linked to transcriptional activation and specifically DNA repair...
Histone deacetylation, the process by which histone deacetylase (HDAC) catalyzes the removal of the acetyl functional group from histones, can be investigated using HDAC antibodies. Decreased levels of acetylation as a result of HDAC activity has been linked to repression of gene expression due to the condensed state of chromatin, referred to as heterochromatin.
Histone acetylation is a crucial component to the regulation of gene expression and impacts the structure of chromatin by tightening it to form heterochromatin or relaxing it to form euchromatin. These varying states impact the level of transcription and numerous cellular processes. Various histone acetylation antibodies can be used for epigenetic research into histone acetylation and gene regulation.