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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Acetyl-Histone H3 (Lys18) Antibody 9675 40 µl
Western Blotting Immunohistochemistry Chromatin Immunoprecipitation
H M R 17 Rabbit 
Histone H3 (D1H2) XP® Rabbit mAb 4499 40 µl
Western Blotting Immunohistochemistry Immunofluorescence Flow Cytometry
H M R Mk 17 Rabbit IgG
Acetyl-Histone H3 (Lys9) (C5B11) Rabbit mAb 9649 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M Z Ce 17 Rabbit IgG
Acetyl-Histone H3 (Lys14) (D4B9) Rabbit mAb 7627 40 µl
Western Blotting Immunoprecipitation Chromatin Immunoprecipitation
H M R Mk 17 Rabbit IgG
Acetyl-Histone H3 (Lys27) (D5E4) XP® Rabbit mAb 8173 40 µl
Western Blotting Immunofluorescence Chromatin Immunoprecipitation
H M R Mk 17 Rabbit IgG
Acetyl-Histone H3 (Lys56) Antibody 4243 40 µl
Western Blotting
H M R Mk 17 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Acetyl-Histone H3 Antibody Sampler Kit provides a fast and economical means of evaluating the acetylation sites on Histone H3. The kit contains enough primary and secondary antibodies to perform four Western mini-blot experiments.


Specificity / Sensitivity

All antibodies in the Acetyl-Histone H3 Antibody Sampler Kit recognize histone H3 only when modified at the indicated site.


Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with synthetic acetylated peptides corresponding to residues surrounding Lys18 or Lys56 of human Histone H3. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding acetylated Lys27 of human histone H3 protein, acetylated Lys14 of human Histone H3 protein, or the amino terminus of histone H3 in which Lys9 is acetylated.

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).


1.  Workman, J.L. and Kingston, R.E. (1998) Annu Rev Biochem 67, 545-79.

2.  Hansen, J.C. et al. (1998) Biochemistry 37, 17637-41.

3.  Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41-5.

4.  Cheung, P. et al. (2000) Cell 103, 263-71.

5.  Bernstein, B.E. and Schreiber, S.L. (2002) Chem Biol 9, 1167-73.

6.  Jaskelioff, M. and Peterson, C.L. (2003) Nat Cell Biol 5, 395-9.

7.  Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13.

8.  Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60.

9.  Goto, H. et al. (1999) J Biol Chem 274, 25543-9.

10.  Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85.

11.  Dai, J. et al. (2005) Genes Dev 19, 472-88.


Entrez-Gene Id 8350
Swiss-Prot Acc. P68431

Protein Specific References

Zhong S et al. (2001) J Biol Chem 276, 33213–9

Li F et al. (2002) EMBO Rep 3, 767–73

Li J et al. (2002) J Biol Chem 277, 49504–10

Sugiyama K et al. (2002) Oncogene 21, 3103–11

Martens JH et al. (2003) Mol Cell Biol 23, 1808–16

Espino PS et al. (2006) Cancer Res 66, 4610–6

Park JH et al. (2006) Cancer Res 66, 9186–95

Soncini C et al. (2006) Clin Cancer Res 12, 4080–9

Idikio HA and (2006) Anticancer Res 26, 4687–94

Wang GG et al. (2007) Nat Cell Biol 9, 804–12

Duan Q et al. (2008) J Biol Chem 283, 33585–90

Dawson MA et al. (2009) Nature 461, 819–22

Cheng MF et al. (2009) Histol Histopathol 24, 1105–11

Hurd PJ et al. (2009) J Biol Chem 284, 16575–83

McGinty RK et al. (2009) ACS Chem Biol 4, 958–68

Banck MS et al. (2009) Epigenetics 4, 100–6

Wu Y et al. (2010) BMC Cancer 10, 32

Pasini D et al. (2010) Nucleic Acids Res 38, 4958–69

Sakabe K and Hart GW (2010) J Biol Chem 285, 34460–8

Gehani SS et al. (2010) Mol Cell 39, 886–900

Jung HR et al. (2010) Mol Cell Proteomics 9, 838–50

Davies GF et al. (2010) Cancer Lett 288, 236–50

Aguilera C et al. (2011) Nature 469, 231–5

Huertas D et al. (2012) Oncogene 31, 1408–18

Joosten M et al. (2013) Haematologica 98, 247–54

Sayegh J et al. (2013) J Biol Chem 288, 9408–17

Dai, J. et al. (2005) Genes Dev 19, 472-88.

Zhong S et al. (2001) J Biol Chem 276, 33213–9

Li F et al. (2002) EMBO Rep 3, 767–73

Li J et al. (2002) J Biol Chem 277, 49504–10

Sugiyama K et al. (2002) Oncogene 21, 3103–11

Martens JH et al. (2003) Mol Cell Biol 23, 1808–16

Espino PS et al. (2006) Cancer Res 66, 4610–6

Park JH et al. (2006) Cancer Res 66, 9186–95

Soncini C et al. (2006) Clin Cancer Res 12, 4080–9

Idikio HA and (2006) Anticancer Res 26, 4687–94

Wang GG et al. (2007) Nat Cell Biol 9, 804–12

Duan Q et al. (2008) J Biol Chem 283, 33585–90

Dawson MA et al. (2009) Nature 461, 819–22

Cheng MF et al. (2009) Histol Histopathol 24, 1105–11

Hurd PJ et al. (2009) J Biol Chem 284, 16575–83

McGinty RK et al. (2009) ACS Chem Biol 4, 958–68

Banck MS et al. (2009) Epigenetics 4, 100–6

Wu Y et al. (2010) BMC Cancer 10, 32

Pasini D et al. (2010) Nucleic Acids Res 38, 4958–69

Sakabe K and Hart GW (2010) J Biol Chem 285, 34460–8

Gehani SS et al. (2010) Mol Cell 39, 886–900

Jung HR et al. (2010) Mol Cell Proteomics 9, 838–50

Davies GF et al. (2010) Cancer Lett 288, 236–50

Aguilera C et al. (2011) Nature 469, 231–5

Huertas D et al. (2012) Oncogene 31, 1408–18

Joosten M et al. (2013) Haematologica 98, 247–54

Sayegh J et al. (2013) J Biol Chem 288, 9408–17

Dai, J. et al. (2005) Genes Dev 19, 472-88.

Zhong S et al. (2001) J Biol Chem 276, 33213–9

Li F et al. (2002) EMBO Rep 3, 767–73

Li J et al. (2002) J Biol Chem 277, 49504–10

Sugiyama K et al. (2002) Oncogene 21, 3103–11

Martens JH et al. (2003) Mol Cell Biol 23, 1808–16

Espino PS et al. (2006) Cancer Res 66, 4610–6

Park JH et al. (2006) Cancer Res 66, 9186–95

Soncini C et al. (2006) Clin Cancer Res 12, 4080–9

Idikio HA and (2006) Anticancer Res 26, 4687–94

Wang GG et al. (2007) Nat Cell Biol 9, 804–12

Duan Q et al. (2008) J Biol Chem 283, 33585–90

Dawson MA et al. (2009) Nature 461, 819–22

Cheng MF et al. (2009) Histol Histopathol 24, 1105–11

Hurd PJ et al. (2009) J Biol Chem 284, 16575–83

McGinty RK et al. (2009) ACS Chem Biol 4, 958–68

Banck MS et al. (2009) Epigenetics 4, 100–6

Wu Y et al. (2010) BMC Cancer 10, 32

Pasini D et al. (2010) Nucleic Acids Res 38, 4958–69

Sakabe K and Hart GW (2010) J Biol Chem 285, 34460–8

Gehani SS et al. (2010) Mol Cell 39, 886–900

Jung HR et al. (2010) Mol Cell Proteomics 9, 838–50

Davies GF et al. (2010) Cancer Lett 288, 236–50

Aguilera C et al. (2011) Nature 469, 231–5

Huertas D et al. (2012) Oncogene 31, 1408–18

Joosten M et al. (2013) Haematologica 98, 247–54

Sayegh J et al. (2013) J Biol Chem 288, 9408–17

Dai, J. et al. (2005) Genes Dev 19, 472-88.


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U.S. Patent No. 5,675,063.