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Anti-trimethyl(Lys9)-phospho(Ser10)-Histone H3
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REFERENCES
A novel role for the Aurora B kinase in epigenetic marking of silent chromatin in differentiated postmitotic cells.
Sabbattini, Pierangela, et al. (2007) EMBO J., 26: 4657-69 (2007)
Binary switches and modification cassettes in histone biology and beyond.
Fischle, Wolfgang, et al. (2003) Nature, 425: 475-9 (2003)
Species Reactivity Key Applications Host Format Antibody Type
H WB, PIA, DB, Mplex Rabbit Culture Supernatant Monoclonal Antibody
Description:
Anti-trimethyl(Lys9)-phospho(Ser10)-Histone H3 Antibody, rabbit monoclonal
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Specificity:
Recognizes histone H3 containing the dual modifications of trimethylation of Lys9 and phosphorylation of Ser10. Does not detect single modifications or other dual modifications of histone H3.
Molecular Weight:
~17 kDa
Epitope:
trimethyl (Lys9)-phospho (Ser10)
Immunogen:
KLH-conjugated, synthetic peptide containing the sequence …ARme3KpST… in which me3K corresponds to trimethyl-lysine 9 and pS to phosphoserine 10 of human histone H3.
Modifications:
Methylation
Phosphorylation
Isotype:
IgG
Background Information:
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pairs of DNA are wrapped around the octamer, forming a nucleosome, the basic subunit of chromatin. Histone modifications regulate DNA transcription, repair, recombination, and replication. These modifications can alter local chromatin architecture, or recruit trans-acting factors that recognize specific histone modifications (the "histone code" hypothesis). Trimethylation of histone H3 on Lys9 (H3K9me3) is one of the most highly studied epigenetic marks. H3K9me3 functions in the repression of euchromatic genes, and in epigenetic control of heterochromatin assembly, most likely via acting as a recognition motif for the binding of chromatin-associated proteins, such as Swi6 or HP1α/β. Phosphorylated Ser10 is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition, Ser10 phosphorylation is also an essential regulatory mechanism for neoplastic cell transformation.
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Species Reactivity:
Human
Species Reactivity Note:
Human. Broad species cross-reactivity is expected, based on sequence homology.
Application Notes:
Peptide Dot Blot Analysis: 1:500 to 1:1,000 dilutions of this antibody only detected histone H3 peptides containing the dual modifications of trimethyl-lysine/phosphoserine at residues 9/10. Peptides containing single or other dual modifications were not detected.
Beadlyte® Histone Peptide Assay: 1:1,000 to 1:2,000 dilutions of this antibody only detected histone H3 peptides containing the dual modifications of trimethyl-lysine/phosphoserine at residues 9/10.
Peptide Inhibition Analysis: 1 μM of histone H3 peptide containing trimethyl-lysine 9/phospho-serine 10 abolished detection of histone H3 by anti-trimethyl (Lys9)-phospho (Ser10)-Histone H3 (1:20,000 dilution) in immunoblots of colcemid-treated HeLa acid extracts.
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Control:
Colcemid treated HeLa cells
Quality Assurance:
Evaluated by Western Blot on HeLa cells.
Western Blotting Analysis: A 1:1000-1:2000 dilution of this antibody detected trimethyl-lysine9-phosphoserine 10 Histone H3 in acid-extracted proteins from HeLa cells treated with colcemid (Figure A).
Presentation:
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