Acetyl lysine plays important roles in gene regulation as a modification of histone proteins, which are responsible for packaging DNA into chromatin. These modifications, in turn, influence the accessibility of DNA to transcription factors and other regulatory proteins, ultimately determining whether a gene is activated or repressed. One of the best-studied roles of acetyl lysine in gene regulation is in gene activation. For example, the histone H3 lysine 9 (H3K9) and histone H3 lysine 27 (H3K27) acetylation marks are associated with gene activation. When these lysine residues are acetylated in histone H3, they weaken the electrostatic interactions between histones and DNA, leading to a more open chromatin structure, allowing binding of transcription factors and RNA polymerase, and promoting gene transcription. For example, acetylation of H3K9 and H3K27 is essential for the activation of genes involved in cell proliferation and differentiation during embryonic development and mutations or dysregulation of these marks can lead to developmental disorders. Acetyl lysine modifications are often enriched at enhancer and promoter regions of genes. Enhancers are the regulatory elements that control gene expression by recruiting transcription factors and other co-regulators. Histone acetylation at these regions enhances the recruitment of transcription factors and co-activators, promoting the formation of transcriptional initiation complexes. In the context of embryonic stem cells, acetylation of lysine 27 on histone H3 (H3K27ac) is a hallmark of active enhancers and promoters, driving the expression of genes involved in pluripotency and self-renewal. Acetyl lysine marks on histones can be heritable through cell divisions, contributing to epigenetic memory, meaning that the state of chromatin can be passed on to daughter cells, ensuring the persistence of specific gene expression patterns across generations. In stem cells, specific acetylation patterns on histones are maintained to preserve pluripotency. For instance, H3K27ac and H3K4me3 are retained on key regulatory genes to ensure their rapid activation upon differentiation cues. Acetyl lysine modifications are dynamic and can be rapidly altered in response to environmental stimuli, allowing cells to adjust their gene expression profiles to adapt to changing environmental conditions. For example, in response to a viral infection, immune cells can rapidly acetylate histones associated with genes involved in antiviral responses. This acetylation facilitates the rapid activation of these genes, assisting the immune system mount a defence against the viral pathogen. Dysregulation of histone acetylation, including acetyl lysine marks, is associated with various diseases. For example, in cancer, aberrant histone acetylation can lead to the activation of oncogenes or the silencing of tumour suppressor genes. In acute myeloid leukaemia (AML), mutations in genes encoding epigenetic regulators can lead to abnormal histone acetylation patterns and these changes are thought to contribute to the uncontrolled proliferation of leukaemic cells. The role of acetyl lysine in gene regulation has led to the development of epigenetic therapies, particularly histone deacetylase inhibitors (HDACIs) which aim to alter acetylation patterns and restore normal gene expression in disease states by tumour suppressor reactivation in cancer. Thus, HDACIs are clinically used in the treatment of certain types of lymphomas and multiple myeloma. We offer a comprehensive product range of research tools for investigating acetyl lysine, including Brd4 antibodies. Explore our full acetyl lysine product range below and discover more, for less.