|Reactivity||Human, Mouse, Rat|
|Calculated MW||15508 Da|
|Other Names||Histone H31t, H3/t, H3t, H3/g, HIST3H3, H3FT|
|Target/Specificity||A synthetic (Dimethyl-K)-peptide corresponding to residues surrounding Lys9 of Histone H3 was used as immunogen. The antibody only detects Histone H3 dimethylated on Lysine 9. Predicted to cross-react with most species, based on sequence homology.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Histone-H3 Antibody Dimethyl (K9) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.|
|Cellular Location||Nucleus. Chromosome.|
|Tissue Location||Expressed in testicular cells.|
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Provided below are standard protocols that you may find useful for product applications.
Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Various post-translational modifications, such as acetylation and methylation, of core histones serve as regulators of gene expression (2). Histone H3 is primarily acetylated at lysines 9, 14, 18, and 23 (3,4). Methylation also serves as a predominant form of post-translational modification of Histone H3, and has been linked to transcriptional regulation and epigenetic silencing via heterochromatin assembly (5). Lysines 4, 9 and 27 in the N-terminal tail of Histone H3 are the preferred sites of methylation.
1. Braunstein, M., et al. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16: 4349
2. Workman, J.L. and R.E. Kingston. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67: 545
3. Hansen, J.C. et al. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37, 17637
4. Strahl, B.D. and C.D. Allis. The language of covalent histone modifications. Nature 403, 41
5. Rice, J.C., and C.D. Allis. Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr Opin Cell Biol. 13: 263
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