Di-Methyl-Histone H3 Antibody Sampler Kit #9847
Product Information
Kit Usage Information
Protocols
- 2901: Western Blotting, Immunohistochemistry (Paraffin), Immunofluorescence*, Flow
- 4499: Western Blotting, Immunohistochemistry (Paraffin), Immunofluorescence*, Flow
- 4658: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence, Flow, ChIP Magnetic, Chromatin IP-seq, CUT&Tag
- 5427: Western Blotting, ChIP Magnetic
- 7074: Western Blotting
- 9725: Western Blotting, Immunoprecipitation (Magnetic), Immunohistochemistry (Paraffin), Immunofluorescence, Flow, ChIP Magnetic, Chromatin IP-seq, CUT&RUN Assay, CUT&Tag
- 9728: Western Blotting, Immunoprecipitation (Magnetic), Immunofluorescence, Flow, ChIP Magnetic
Product Description
Specificity / Sensitivity
All antibodies in the Di-Methyl-Histone H3 Antibody Sampler Kit recognize histone H3 only when modified at the indicated site.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic di-methylated peptides corresponding to residues surrounding Lys 4 of human Histone H3. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with synthetic di-methylated peptides corresponding to residues surrounding Lys 9, 27, 36 and 79 of human Histone H3. Histone H3 (D1H2) XP Rabbit mAb is produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of the human histone H3 protein.
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). 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).
- Peterson, C.L. and Laniel, M.A. (2004) Curr Biol 14, R546-51.
- Kubicek, S. et al. (2006) Ernst Schering Res Found Workshop, 1-27.
- Lin, W. and Dent, S.Y. (2006) Curr Opin Genet Dev 16, 137-42.
- Lee, D.Y. et al. (2005) Endocr Rev 26, 147-70.
- Daniel, J.A. et al. (2005) Cell Cycle 4, 919-26.
- Shi, X. et al. (2006) Nature 442, 96-9.
- Wysocka, J. et al. (2006) Nature 442, 86-90.
- Wysocka, J. et al. (2005) Cell 121, 859-72.
- Trojer, P. and Reinberg, D. (2006) Cell 125, 213-7.
Limited Uses
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