|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||11367 Da|
|Other Names||Histone H4, HIST1H4A, H4/A, H4FA|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Histone H4 was used as an immunogen.|
|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-H4 Antibody Acetyl (K5) 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.|
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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 histone H4 thus appears to play a primary role in the structural changes that mediate enhanced binding of transcription factors to their recognition sites within nucleosomes (3). Histone H4 can be reversibly acetylated at lysine residues 5, 8, 12 and 16. It has been shown that, in H4 from human cells, the four lysine residues are acetylated in a preferred, but not exclusive order, namely lysine 16, followed by 12 and 8, followed by 5 (4).
1. Braunstein M, et al. Mol. Cell. Biol. 16:4349
2. Workman JL, et al, Annu. Rev. Biochem. 67: 545
3. Vettese-Dadey M., et al. EMBO J 15(10):2508-18, 1996
4. Turner BM, et al. FEBS Lett 253(1-2):141-5, 1989
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