| CatalogCode: | NB100-2210 |
| ProductName: | Histone H3 Antibody |
| Product Description: | Rabbit Polyclonal anti-Histone H3 |
| Clonality: | Polyclonal |
| Immunogen: | Synthetic peptide corresponding to amino acids 7-20 of Histone H3 conjugated to KLH. |
| Specificity: | Detects a band at approximately 17kDa. There is no inhibition with non-acetylated Histone H3 peptide. This histone H3 sequence is identical in many species including mouse, rat, bovine, chicken, frog, drosophila, and C. elegans. |
| CrossReactivity: | Cross-reacts with Human. Expected to cross-react with mouse, rat, bovine, chicken, frog, drosophila, and C. elegans. |
| Packaging: | 0.1 ml |
| Uses: | WB: Use at a dilution of 1/1,000. IF: Use at a dilution of 1/1,000. Not tested in any other applications. Optimal dilution should be determined by the end user. |
| Control: | Mouse fibroblast NIH3T3 cells treated with sodium butyrate. |
| Background: | Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higherorder chromatin fibers.1,2 The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. The relatively unstructured and highly chargedN-terminal tail domains of histones, are central to the processes that modulate chromatin structure. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones.3,4 In addition, ATPdriven remodeling complexes, such as SWI/SNF, alter chromatin conformation.5,6 These modifications alter chromatin structure by influencing histone-DNA and histone-histone interactions, and provide an exposed surface for the potential interaction of the tail domain with other proteins involved in transcription regulation. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation.2,7 This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23.3,8-11 Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.8,12,13 Acetylation of specific lysine residues in H3 is also associated with processes apart from transcription. During DNA replication, new histones are rapidly synthesized and assembled onto replicated DNA. Histones H3 and H4 are brought to replicating chromatin in a pre-acetylated state that turns into a de-acetylated state after replication is completed and the newly assembled chromatin matures. |
| Storage: | Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze thaw cycles. |
| Purity: | Immunogen affinity purified |
| Host_Name: | Rabbit |
| Buffer: | 0.01M PBS, pH 7.4 containing 15mM sodium azide |
| ListPrice: | 295 |
| AppSummary: | WB, IF |
| SpeciesSummary: | Hu |
| ALTnames: | anti-H3 antibody, anti-HisH3 antibody, anti-His1H3 antibody, anti-H3/a antibody, anti-H3/b antibody, anti-H3 antibody, anti-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-Histone H3 antibody |
| ProteinTarget: | Histone H3 |
| PackageSize: | 0.1 ml |
| GeneralRef: | 1. Luger, K., and Richmond, T.J., Curr. Opin. Genet. Dev., 8, 140 (1998). 2. Kornberg, R.D., and Lorch, Y., Cell, 98, 285 (1999). 3. Strahl, B.D., and Allis, C.D., Nature, 403, 41 (2000). 4. Cheung, P., et al., Cell, 103, 263 (2000). 5. Krebs, J.E., et al., Cell, 102, 587 (2000). 6. Fry, C.J., and Peterson, C.L., Science, 295, 1847 (2002). 7. Struhl, K., Genes Dev., 12, 599 (1998). 8. Turner, B.M., and O'Neill, L.P., Semin. Cell. Biol., 6, 229 (1995). 9. Thorne, A.W., et al., Eur. J. Biochem., 193, 701 (1990). 10. Grant, P.A., et al., J. Biol. Chem., 274, 5895 (1999). 11. Zhang, W., et al., EMBO J., 17, 3155 (1998). 12. Kuo, M.H., et al., Nature, 383, 269 (1996). 13. Sobel, R.E., et al., Proc. Natl. Acad. Sci. USA, 92, 1237 (1995). |
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