Product Pathways - Chromatin Regulation

Histone Deacetylase (HDAC) Antibody Sampler Kit #9928

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Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey

Specificity / Sensitivity

The Histone Deacetylase (HDAC) Antibody Sampler Kit provides a fast and economical means to evaluate the endogenous levels of HDACs. The kit contains enough primary and secondary antibodies to perform four mini-blot experiments.Each antibody in the Histone Deacetylase (HDAC) Antibody Sampler Kit detects endogenous levels of its target and does not recognize other family members.

Western Blotting

Western blot analysis of extracts from COS and HeLa cells using Histone Deacetylase 1 (HDAC1) Antibody #2062.

Western Blotting

Western blot analysis of lysates from various cell lines or tissues using Histone Deacetylase 4 (HDAC4) Antibody #2072.

Western Blotting

Western blot analysis of lysates from various cell lines using Histone Deacetylase 5 (HDAC5) Antibody #2082.

Western Blotting

Western blot analysis of various cell types using HDAC2 Antibody #2540.

Western Blotting

Western blot analysis of extracts COS and HeLa cells using Histone Deacetylase 3 (HDAC3) Antibody #2632.

Western Blotting

Western blot analysis of extracts from COS aand HeLa cells using Histone Deacetylase 7 (HDAC7) Antibody #2882.

IHC-P (paraffin)

Immunohistochemical staining of paraffin-embedded human tonsil, showing nuclear localization of HDAC5, using Histone Deacetylase 5 (HDAC5) Antibody #2082.

IHC-P (paraffin)

Immunohistochemical staining of paraffin-embedded human breast carcinoma, showing nuclear localization of HDAC3, using Histone Deacetylase 3 (HDAC3) Antibody #2632.

IC-ABC

Immunocytochemical staining of HeLa cells, using Histone Deacetylase 1 (HDAC1) Antibody #2062 (left) or the same antibody preincubated with HDAC1 peptide (right).

IC-ABC

Immunocytochemical staining of NIH/3T3 cells, using Histone Deacetylase 3 (HDAC3) Antibody #2632 (left) or the same antibody preincubated with specific HDAC3 peptide (right).

IC-ABC

Immunocytochemical staining of C6 cells, using Histone Deacetylase 7 (HDAC7) Antibody #2882 (left) or the same antibody preincubated with specific HDAC7 peptide (right).

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with synthetic (KLH-coupled) corresponding to the amino-terminal residues of HDAC1, -5 and -6 and to the carboxy-terminal residues of HDAC3, -4 and -7. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing trans factors increased accessibility to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate non-histone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I (HDACs 1, 2, 3 and 8) proteins are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9 and 10) are related to yeast Hda1-like proteins and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

1. Marmorstein, R. et al. (2001) Cell. Mol. Life Sci. 58, 693-703.
2. Gregory, P.D. et al. (2001) Exp. Cell Res. 265, 195-202.
3. Liu, Y. et al. (2000) Mol. Cell. Biol. 20, 5540-5543.
4. Cress, S.D. and Seto, E. (2000) J. Cell. Physiol. 184, 1-16.
5. Gray, S.G. and Ekstrom, T.J. (2001) Exp. Cell Res. 262, 75-83.
6. Thiagalingam, S. et al. (2003) Ann. N. Y. Acad. Sci. 983, 84-100.
7. Viguishin, D.M. and Coombes, R.C. (2004) Curr. Cancer Drug Targets 4, 205-218.

Application References

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