Phospho-Histone H3 (Thr11) Ant

9764:

Flow , Immunofluorescence , Immunoprecipitation , Western Blotting

Phospho-Histone H3 (Thr11) Antibody detects endogenous levels of histone H3 only when phosphorylated at threonine 11. The antibody does not cross-react with other phosphorylated histones or with acetylated histones.

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr11 of human histone H3. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of lysates from HeLa, C6 and NIH/3T3 cells treated for 24 hours with or without nocodazole and also with or without λ phosphatase, using Phospho-Histone H3 (Thr11) Antibody #9764 (upper) or Histone H3 Antibody #9715 (lower).

Flow Cytometry

Flow cytometric analysis of untreated Jurkat cells, using Phospho-Histone H3 (Thr11) Antibody versus propidium iodide (DNA content). The boxed population indicates Phospho-Histone H3 (Thr11)-positive cells.

IF-IC

Confocal immunofluorescent analysis showing positive signal in mitotic HeLa cells, using Phospho-Histone H3 (Thr11) Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red).

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).

1. Workman, J.L. and Kingston, R.E. (1998) Annu Rev Biochem 67, 545-79.
2. Hansen, J.C. et al. (1998) Biochemistry 37, 17637-41.
3. Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41-5.
4. Cheung, P. et al. (2000) Cell 103, 263-71.
5. Bernstein, B.E. and Schreiber, S.L. (2002) Chem Biol 9, 1167-73.
6. Jaskelioff, M. and Peterson, C.L. (2003) Nat Cell Biol 5, 395-9.
7. Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13.
8. Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60.
9. Goto, H. et al. (1999) J Biol Chem 274, 25543-9.
10. Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85.
11. Dai, J. et al. (2005) Genes Dev 19, 472-88.
12. Hepatology. 2008 Jun;47(6):2036-50

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For Research Use Only. Not For Use In Diagnostic Procedures.