Histone H3K27me3 AntibodyСпецификацияОбъем | 100 мкл | Синонимы | HIST1H3J, H3/j, H3FJ, Histone H3.1, Histone H3/a, Histone H3/b, Histone H3/c, Histone H3/d, Histone H3/f, Histone H3/h, Histone H3/I, HistoneH3/j, Histone H3/k, Histone H3/l, HIST3H3, | Клональность | Polyclonal Antibody | Организм | Human | uniprot | Q16695 | Иммуноген | A synthetic methylated peptide corresponding to residues surrounding K27 of human histone H3 | Источник | Rabbit | Видовая специфичность | Human, Mouse, Rat | Применение | ELISA, WB, IHC, IF, IP, ChIP,WB:1:500-1:2000, IHC:1:50-1:200, IF:1:50-1:200, IP:1:50-1:200, ChIP:1:50-1:200 | Примечание | Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).</p><div> ,</div><div style=margin-right:9.45pt,line-height:115%">1. Workman, J.L. and Kingston, R.E. (1998) Annu Rev Biochem 67, 545-79.</div><div style="margin-right:9.45pt,line-height:115%">2. Hansen, J.C. et al. (1998) Biochemistry 37, 17637-41.</div><div style="margin-right:9.45pt,line-height:115%">3. Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41-5.</div><div style="margin-right:9.45pt,line-height:115%">4. Cheung, P. et al. (2000) Cell 103, 263-71.</div><div style="margin-right:9.45pt,line-height:115%">5. Bernstein, B.E. and Schreiber, S.L. (2002) Chem Biol 9, 1167-73.</div><div style="margin-right:9.45pt,line-height:115%">6. Jaskelioff, M. and Peterson, C.L. (2003) Nat Cell Biol 5, 395-9.</div><div style="margin-right:9.45pt,line-height:115%">7. Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13.</div><div style="margin-right:9.45pt,line-height:115%">8. Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60.</div><div style="margin-right:9.45pt,line-height:115%">9. Goto, H. et al. (1999) J Biol Chem 274, 25543-9.</div><div style="margin-right:9.45pt,line-height:115%">10. Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85.</div><div style="margin-right:9.45pt,line-height:115%">11. Dai, J. et al. (2005) Genes Dev 19, 472-88.</div>" | Клональность1 | Polyclonal | Изотип | IgG | Коньюгат | Non-conjugated | Буффер | Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. | Форма | liquid | Хранение | Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. | Метод очистки | Antigen Affinity Purified | Абревеатура | K27me3 | Области исследований | Epigenetics and Nuclear Signaling | Ссылка на страницу на сайте производителя | ссылка | Western blot analysis of extracts of HeLa cell line and H3 protein expressed in E.coli., using H3K27me3antibody.
| Dot-blot analysis of all sorts of methylation peptides using H3K27me3 antibody.
| Immunofluorescence analysis of 293T cell using H3K27me3 antibody. Blue: DAPI for nuclear staining.
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