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Acetyl-Histone H3 (Lys23) Antibody #8848
This product is discontinued
Acetyl-Histone H3 (Lys23) Antibody specificity was determined by peptide ELISA. The graph depicts the binding of the antibody to pre-coated acetyl-histone H3 (Lys23) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the acetyl-histone H3 (Lys23) peptide competed away binding of the antibody.Learn more about how we get our images
Gallery: Acetyl-Histone H3 (Lys23) Antibody #8848
Acetyl-Histone H3 (Lys23) Antibody recognizes endogenous levels of histone H3 protein only when acetylated at Lys23. This antibody does not cross-react with histone H3 acetyl-lysine 9, 14, 18, 27, or 56.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding acetyl-Lys23 of human histone H3 protein. Antibodies are purified by protein A and peptide affinity chromatography.
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).
For Research Use Only. Not For Use In Diagnostic Procedures. Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.