Product Pathways - Chromatin Regulation / Epigenetics
Histone H3 (D1H2) XP® Rabbit mAb (Biotinylated) #5748
|5748S||100 µl (10 western blots)||---||In Stock||---|
|5748||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||17||Rabbit IgG|
Species cross-reactivity is determined by western blot using the unconjugated antibody.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Hamster, Chicken, D. melanogaster, Xenopus, Zebrafish, Bovine.
Specificity / Sensitivity
Histone H3 (D1H2) XP® Rabbit mAb (Biotinylated) detects endogenous levels of total histone H3 protein, including the Histone H3 variant CENP-A. This antibody does not cross-react with other core histones.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of the human histone H3 protein.
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Histone H3 (D1H2) XP® Rabbit mAb #4499.
Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of 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, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 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 (8-10). Phosphorylation at 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 at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).
- Workman, J.L. and Kingston, R.E. (1998) Annu Rev Biochem 67, 545-79.
- Hansen, J.C. et al. (1998) Biochemistry 37, 17637-41.
- Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41-5.
- Cheung, P. et al. (2000) Cell 103, 263-71.
- Bernstein, B.E. and Schreiber, S.L. (2002) Chem Biol 9, 1167-73.
- Jaskelioff, M. and Peterson, C.L. (2003) Nat Cell Biol 5, 395-9.
- Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13.
- Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60.
- Goto, H. et al. (1999) J Biol Chem 274, 25543-9.
- Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85.
- Dai, J. et al. (2005) Genes Dev 19, 472-88.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
XP is a trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.