Acetylation is a common post-translational modification of histone proteins catalysed by chromatin modifying enzymes termed histone acetyltransferases (HATs) or histone acetylases. This reversible modification involves the addition of an acetyl group (CH3CO-) to specific lysine residues on histone tails, influencing chromatin structure and gene expression. Acetylation of histones neutralizes their positive charge, thereby weakening their interaction with negatively charged DNA. This results in chromatin de-condensation, making the DNA more accessible to transcription factors and other regulatory proteins, facilitating gene transcription. Acetylation of specific histone lysine residues, such as H3K9 and H3K14, is strongly associated with such gene activation. Such acetylation marks on promoter regions and enhancers promotes the recruitment of the transcriptional machinery and facilitates the binding of transcription factors to DNA, leading to increased gene expression. Acetylation at enhancer regions is also critical for gene activation, allowing the assembly of transcriptional enhancer complexes that promote gene expression. For example, acetylation of H3K27 is associated with active gene enhancers. Acetylation patterns on histones can be inherited through cell divisions, providing a form of epigenetic memory. This memory helps maintain cell identity and regulate tissue-specific gene expression. Histone Acetyltransferases (HATs) are enzymes responsible for adding acetyl groups to histone lysine residues. They include families like the p300/CBP family, the GNAT family (e.g., GCN5 and PCAF), and the MYST family (e.g., MOF and Tip60). HATs catalyse acetylation by transferring the acetyl group from acetyl-coenzyme A (acetyl-CoA) to histone lysine residues. HATs often function as part of larger co-activator complexes. For example, the p300/CBP co-activator complex recruits HAT activity to specific gene promoters, enhancing transcriptional activation. Similarly, the SAGA complex incorporates the GCN5 HAT to modify chromatin in a gene-specific manner. Proteins containing bromodomains can read the acetylation marks on histones and facilitate the recruitment of other transcriptional machinery, further enhancing gene expression. For example, BRD4 recognizes acetylated histones and helps initiate transcriptional elongation. The p300 and CBP (CREB-binding protein) co-activators are essential for acetylation at specific lysine residues on histones H3 and H4. They play a critical role in the regulation of numerous genes involved in cell differentiation, development, and responses to external stimuli. Dysregulation of p300/CBP activity has been implicated in various diseases, including cancer. GCN5 and PCAF are members of the GNAT family of HATs. They are involved in nucleosome remodelling by acetylating histones within nucleosomes, leading to chromatin relaxation and gene activation. This process is crucial for gene expression during development and cellular responses to environmental cues. Tip60, a member of the MYST family of HATs, also plays a vital role in the DNA damage response. It acetylates histone H4, and other factors involved in DNA repair, promoting the recruitment of repair proteins to damaged sites, facilitating efficient DNA repair. Thus, acetylation by chromatin modifying enzymes is a critical epigenetic modification that plays roles in regulating gene expression and chromatin structure. Histone acetyltransferases (HATs) add acetyl groups to histones, leading to chromatin relaxation and gene activation. We offer a wide product catalogue of research reagents for investigating acetylation, including HDAC3 antibodies, HDAC6 antibodies, HDAC1 antibodies, HDAC6 ELISA Kits, and SIRT1 ELISA Kits. Explore our full acetylation product range below and discover more, for less. Alternatively, you can explore our HDACs and HAT product ranges.