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Tri-Methyl-Histone H3 (Lys27) Antibody #9756
This product is discontinued
Tri-Methyl-Histone H3 (Lys27) Antibody specificity was determined by peptide ELISA. The graphs depict the binding of the antibody to pre-coated tri-methyl histone H3 (Lys27) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the tri-methyl histone H3 (Lys27) peptide competed away binding of the antibody.Learn more about how we get our images
Gallery: Tri-Methyl-Histone H3 (Lys27) Antibody #9756
Tri-Methyl-Histone H3 (Lys27) Antibody detects endogenous levels of histone H3 only when tri-methylated on Lys27. The antibody does not cross-react with non-methylated, mono-methylated or di-methylated Lys27. In addition, the antibody does not cross-react with mono-methylated, di-methylated or tri-methylated histone H3 at Lys4, Lys9, Lys36 or Histone H4 at Lys20.Species predicted to react based on 100% sequence homology: Xenopus
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of histone H3 in which Lys27 is tri-methylated. Antibodies are purified by 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). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).
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