| CatalogCode: | NB110-57047 |
| ProductName: | Dimethyl-Histone H3 (Dimethyl-K9) Antibody |
| Product Description: | Rabbit Monoclonal anti-Dimethyl-Histone H3 (Dimethyl-K9) (Y49) |
| Clone: | Y49 |
| Clonality: | Monoclonal |
| Specificity: | A synthetic (Dimethyl-K)-peptide corresponding to residues surrounding Lys9 of Histone H3 was used as immunogen. The antibody only detects Histone H3 dimethylated on Lysine 9. Predicted to cross-react with most species, based on sequence homology. |
| CrossReactivity: | Reacts in human, mouse, and rat. Not tested in other species. |
| Packaging: | 0.1 ml Rabbit ascites. |
| Uses: | WB: 1:1,000ICC: 1:100 |
| Background: | Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Various post-translational modifications, such as acetylation and methylation, of core histones serve as regulators of gene expression (2). Histone H3 is primarily acetylated at lysines 9, 14, 18, and 23 (3,4). Methylation also serves as a predominant form of post-translational modification of Histone H3, and has been linked to transcriptional regulation and epigenetic silencing via heterochromatin assembly (5). Lysines 4, 9 and 27 in the N-terminal tail of Histone H3 are the preferred sites of methylation. |
| Storage: | Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
| Isotype: | IgG |
| Host_Name: | Rabbit |
| Buffer: | 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, and 0.05% BSA. |
| ListPrice: | 325 |
| AppSummary: | WB, ICC |
| SpeciesSummary: | Hu, Mu, Rt |
| ALTnames: | anti-H3 histone antibody, anti-H3/a antibody, anti-H3/b antibody, anti-H3/c antibody, anti-H3/d antibody, anti-h3/f antibody, anti-H3/h antibody, anti-H3/i antibody, anti-H3/j antibody, anti-H3/k antibody, anti-H3/l antibody, anti-H3F3 antibody, anti-HIST3H3 antibody, anti-Histone H 3 antibody |
| PackageSize: | 0.1 ml |
| GeneralRef: | 1. Braunstein, M., et al. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16: 4349-56 (1996). 2. Workman, J.L. and R.E. Kingston. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67: 545-579 (1998). 3. Hansen, J.C. et al. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37, 17637-17641 (1998). 4. Strahl, B.D. and C.D. Allis. The language of covalent histone modifications. Nature 403, 41-45 (2000). 5. Rice, J.C., and C.D. Allis. Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr Opin Cell Biol. 13: 263-73 (2001). |
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