antibody

Histone H3, phosphorylated (Thr11)

H5110-11R2

100 ul

polyclonal

domestic rabbit

nonconjugated

phosphorylated

Histone H3, phosphorylated (Thr11)

rabbit

Pab

Phosphorylated

Antibodies

100 ul

IgG

Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (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, on gene expression (6). In most species, histone H2B is primarily acetylated at lysines 5, 12, 15 and 20 (4,7). Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23 (2,3). Acetylation 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 (8,9,10). Phosphorylation of 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 of H3 Thr3 in prophase and its dephosphorylation during anaphase (11). Applications: Suitable for use in Immunofluorescence, Flow Cytometry, ELISA, Western Blot, Immunoprecipitation. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 Immunoprecipitation: 1:50 Immunofluorescence (IF-IC): 1:100 Flow Cytometry: 1:25 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Hu Mo Rt

Synthetic phosphopeptide corresponding to residues surrounding Thr11 of human histone H3.

Detects endogenous levels of histone H3 only when phosphorylated at threonine 11. Does not crossreact with other phosphorylated histones or with acetylated histones. Species Crossreactivity: human, mouse and rat

Purified by Protein A and peptide affinity chromatography.

Supplied as a liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol.

Not determined

Product Type: Pab Isotype: IgG Host: rabbit Source: human Concentration: Not determined Form: Supplied as a liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol. Purity: Purified by Protein A and peptide affinity chromatography. Immunogen: Synthetic phosphopeptide corresponding to residues surrounding Thr11 of human histone H3. Specificity: Detects endogenous levels of histone H3 only when phosphorylated at threonine 11. Does not crossreact with other phosphorylated histones or with acetylated histones. Species Crossreactivity: human, mouse and rat Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

FC IF IP WB

-20°C

(1) Workman, J.L. and Kingston, R.E. (1998) Annu. Rev. Biochem. 67, 545–579. (2) Hansen, J.C. et al. (1998) Biochemistry 37, 17637–17641. (3) Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41–45. (4) Cheung, P. et al. (2000) Cell 103, 263–271. (5) Bernstein, B.E. and Schreiber, S.L. (2002) Chem. Biol. 9, 1167–1173. (6) Jaskelioff, M. and Peterson, C.L. (2003) Nat. Cell Biol. 5, 395–399. (7) Thorne, A.W. et al. (1990) Eur. J. Biochem. 193, 701–713. (8) Hendzel, M. J. et al. (1997) Chromosoma 106, 348–360. (9) Goto, H. et al. (1999) J. Biol. Chem. 274, 25543–25549. (10) Preuss, U. et al. (2003) Nucleic Acids Res. 31, 878–885. (11) Dai, J. et al. (2005) Genes Dev. 19, 472–488.

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