|Application ||WB, IHC|
|Calculated MW||15508 Da|
|Other Names||Histone H31t, H3/t, H3t, H3/g, HIST3H3, H3FT|
|Target/Specificity||A synthetic phospho-peptide corresponding to residues surrounding Ser28 of human Histone H3 was used as immunogen. The antibody only detects Histone H3 phosphorylated on Serine 28.|
|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 Phospho (pS28) 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). Acetylation of core histones regulates gene expression (2). Histone H3 is primarily acetylated at lysines 9, 14, 18, and 23 (3,4). Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (3,4).
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
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