Bromodomain proteins are a class of epigenetic regulators that have roles in the regulation of gene expression by recognizing and binding to acetylated lysine residues on histone proteins. They are involved in a wide range of cellular processes, including transcriptional activation, DNA repair, and cell cycle regulation. BRD4 (Bromodomain-containing protein 4) is a member of the BET (Bromodomain and Extra-Terminal domain) protein family and is known for its involvement in epigenetic regulation and gene expression. BRD4 is involved in transcriptional regulation via recruitment of the transcriptional machinery to acetylated chromatin regions. BRD4 has been shown to regulate the expression of important cell cycle regulators such as cyclin D1, involved in regulating the G1 phase of the cell cycle. In addition, BRD4 is important in regulating transcriptional elongation helping to maintain the expression of genes, including those related to cell cycle control, by preventing the premature transcriptional termination of RNA polymerase II (RNAPII). In this function, BRD4 interacts with the positive transcription elongation factor b (P-TEFb) facilitating the release of RNA polymerase II from promoter-proximal pausing, allowing for productive transcription elongation. This activity can also stabilize the expression of genes involved in cell cycle progression, ensuring their continuous expression throughout the cell cycle. BRD4 has also been implicated in cancer progression, playing a role in maintaining the expression of oncogenes, and is often overexpressed in various cancers. BRD2 and BRD3 are closely related bromodomain proteins that also play roles in transcriptional regulation. They are involved in the formation of transcriptional complexes and facilitate the recruitment of transcription factors to chromatin, thereby contributing to the maintenance of cell identity and differentiation. A notable function of BRD2 and BRD3 is their involvement in the regulation of inflammatory genes. They promote the expression of pro-inflammatory genes by binding to acetylated histones at their promoters, leading to increased transcription. This has implications for various diseases, including autoimmune disorders. Additionally, BRD2 and BRD3 are associated with cell cycle regulation. In this context they interact with E2F transcription factors and modulate their activity, thereby affecting cell cycle progression. Aside from these specific functions, bromodomain proteins collectively participate in several general cellular processes. For example, bromodomain proteins play a role in the recruitment of repair factors to DNA damage sites, aiding in DNA repair processes, and thereby contributing to genomic stability. For example, the bromodomain-containing protein ATAD2 is involved in DNA repair processes, recognizing acetylated histones at sites of DNA damage, and assisting recruitment of the DNA repair machinery to facilitate repair. This interaction promotes a local chromatin remodelling event that allows repair proteins access to the damaged DNA. They are also involved in other changes to chromatin structure, allowing access to DNA by various regulatory proteins and complexes. For example, some subunits of the SWI/SNF chromatin remodelling complex contain bromodomains which help the SWI/SNF complex bind to acetylated histones and mediate the ATP-dependent repositioning of nucleosomes. This can then facilitate changes in chromatin accessibility and structure, which are essential for transcriptional regulation. We provide a large product range of research tools for studying Bromodomain containing proteins, including Brd4 antibodies. Explore our full Bromodomain containing proteins product range below and discover more, for less.