Phospho-Histone H3 (Thr11) (C2A6) Rabbit mAbProduct information
Phospho-Histone H3 (Thr11) (C2A6) Rabbit mAb
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Chromatin Regulation / Epigenetics
Phospho-Histone H3 (Thr11) (C2A6) Rabbit mAb #9767
|9767S||100 µl (10 western blots)||---||In Stock||---|
|9767||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat||Endogenous||17||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, F=Flow Cytometry
Species predicted to react based on 100% sequence homology: Xenopus.
Specificity / Sensitivity
Phospho-Histone H3 (Thr11) (C2A6) Rabbit mAb detects endogenous levels of histone H3 only when phosphorylated at Thr11. This antibody does not cross-react with other phosphorylated histones.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr11 of human histone H3.
Western blot analysis of lysates from HeLa, NIH/3T3 and C6 cells treated for 24 hours with or without nocodazole (100 ng/ml) and also with or without λ phosphatase, using Phospho-Histone H3 (Thr11) (C2A6) Rabbit mAb (upper) or Histone H3 Antibody #9715 (lower).
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).
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- Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13.
- Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60.
- Goto, H. et al. (1999) J Biol Chem 274, 25543-9.
- Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85.
- Dai, J. et al. (2005) Genes Dev 19, 472-88.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
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U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.