Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

Acetyl-Histone H4 Antibody Sampler Kit #8346

Kit Includes Quantity Applications Reactivity MW (kDa) Isotype
Acetyl-Histone H4 (Lys12) Antibody #2591 40 µl W IF-IC H M R Mk 11 Rabbit
Acetyl-Histone H4 (Lys5) Antibody #9672 40 µl W IP IHC-P IF-IC ChIP H M R Mk (C) (Dm) (X) (Z) (B) (Pg) (Hr) (Ce) 11 Rabbit
Acetyl-Histone H4 (Lys8) Antibody #2594 40 µl W H M R Mk (Ce) 11 Rabbit
Histone H4 (L64C1) Mouse mAb #2935 40 µl W IHC-P H M R Mk Z (Dm) (X) (B) (Hr) (Ce) 11 Mouse IgG1
Anti-rabbit IgG, HRP-linked Antibody #7074 100 µl Goat
Anti-mouse IgG, HRP-linked Antibody #7076 100 µl Horse

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)  ChIP=Chromatin IP
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  Dm=D. melanogaster  X=Xenopus  Z=Zebrafish  B=Bovine  Pg=Pig  Hr=Horse  Ce=C. elegans
Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Specificity / Sensitivity

Each antibody in this kit recognizes only its specific target protein and does not cross-react with other family members.

Western blot analysis of extracts from various cell lines, untreated or TSA-treated (400 nM TSA for 12 hours), using Acetyl-Histone H4 (Lys12) Antibody #2591.

Western blot analysis of extracts from various cell lines, untreated or TSA-treated (400 nM TSA for 12 hours), using Acetyl-Histone H4 (Lys8) Antibody #2594.

Western blot analysis of various cell lines using Histone H4 (L64C1) Mouse mAb #2935.


Western blot analysis of extracts from various cell lines using Acetyl-Histone H4 (Lys5) Antibody #9672.

Description

The Acetyl-Histone H4 Antibody Sampler Kit provides an economical means of detecting total histone H4 as well as histone H4 acetylated at various residues including Lys12, Lys5, and Lys8. The kit contains enough primary and secondary antibody to perform four western blots with each antibody.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic acetylated peptide corresponding to residues surrounding Lys12, Lys5 or Lys8 of human histone H4. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence of human histone H4.

Background

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.

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