CST, 93244C, FastScan™ Acetyl-Histone H3 (Lys27) ELISA Kit

FastScan ELISA Kit for studying H3 (Lys27) acetylate in the research area. Protocol Available protocols: ELISA+ Specificity / Sensitivity The FastScan™ Acetyl-Histone H3 (Lys27) ELISA Kit detects endogenous levels of histone H3 when acetylated at Lys27, as shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species. Species Reactivity: Human, Mouse, Rat, Monkey Background The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A (Lys5), H2B (Lys5, 12, 15, and 20), H3 (Lys9, 14, 18, 23, 27, 36, and 56), and H4 (Lys5, 8, 12, and 16) and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues (6). Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases (HATs), such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation (3). Deacetylation, which is mediated by histone deacetylases (HDAC and sirtuin proteins), reverses the effects of acetylation and generally facilitates transcriptional repression (7,8). Alternate Names H3; H3 clustered histone 1; H3 histone family, member A; H3/A; H31; H3C1; H3C10; H3C11; H3C12; H3C2; H3C3; H3C4; H3C6; H3C7; H3C8; H3FA; H3FB; H3FC; H3FC HIST1H3C; H3FD; H3FF; H3FH; H3FI; H3FJ; H3FK; H3FL; HIST1H3A; HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J; histone 1, H3a; histone cluster 1 H3 family member a; histone cluster 1, H3a; Histone H3; Histone H3.1; Histone H3/a; Histone H3/b; Histone H3/c; Histone H3/d; Histone H3/f; Histone H3/h; Histone H3/i; Histone H3/j; Histone H3/k; Histone H3/l Specification REACTIVITY: H M R Mk