Product Pathways - Chromatin Regulation / Epigenetics
Histone Deacetylase (HDAC) Antibody Sampler Kit #9928
|9928S||1 Kit (6 x 40 µl)||---||In Stock||---|
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|Kit Includes||Quantity||Applications||Reactivity||MW (kDa)||Isotype|
|HDAC1 (10E2) Mouse mAb #5356||40 µl||W, IP, IF-IC||H, M, R, Mk||62||Mouse IgG1|
|HDAC2 (3F3) Mouse mAb #5113||40 µl||W, IP, IF-IC||H, M, R, Mk||60||Mouse IgG1|
|HDAC3 (7G6C5) Mouse mAb #3949||40 µl||W, IP, IF-IC||H, M, R, Mk||49||Mouse IgG2a|
|HDAC4 (D15C3) Rabbit mAb #7628||40 µl||W, IP||H, M, R, Mk||140||Rabbit IgG|
|Histone Deacetylase 5 (HDAC5) Antibody #2082||40 µl||W, IP, IHC-P||H, M, R, Mk||124||Rabbit|
|HDAC6 (D2E5) Rabbit mAb #7558||40 µl||W, IP, IHC-P, IF-IC||H, Mk||160||Rabbit IgG|
|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, IF-IC=Immunofluorescence (Immunocytochemistry), IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key: H=Human, M=Mouse, R=Rat, Mk=Monkey
Western blot analysis of lysates from various cell lines using Histone Deacetylase 5 (HDAC5) Antibody #2082.
Western blot analysis of extracts from various cell lines using HDAC3 (7G6C5) Mouse mAb #3949.
Western blot analysis of extracts from various cell lines using HDAC2 (3F3) Mouse mAb #5113.
Western blot analysis of extracts from HeLa, NIH/3T3, and H-4-II-E cells using HDAC1 (10E2) Mouse mAb #5356.
Western blot analysis of extracts from various cell lines using HDAC6 (D2E5) Rabbit mAb #7558.
Western blot analysis of extracts from various cell lines using HDAC4 (D15C3) Rabbit mAb #7628.
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 Western blot experiments.
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.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to the carboxy terminus of human HDAC5 protein. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with a recombinant protein specific to the carboxy terminus of human HDAC6, the amino terminus of human HDAC4 protein or with synthetic peptides to the carboxy-terminal residues of human HDAC1 and HDAC2 proteins. HDAC3 (7G6C5) monoclonal antibody is produced by immunizing animals with recombinant human HDAC3 protein.
Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors 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 nonhistone 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 proteins (HDACs 1, 2, 3, and 8) 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).
- Marmorstein, R. (2001) Cell Mol Life Sci 58, 693-703.
- Gregory, P.D. et al. (2001) Exp Cell Res 265, 195-202.
- Liu, Y. et al. (2000) Mol Cell Biol 20, 5540-53.
- Cress, W.D. and Seto, E. (2000) J Cell Physiol 184, 1-16.
- Gray, S.G. and Ekström, T.J. (2001) Exp Cell Res 262, 75-83.
- Thiagalingam, S. et al. (2003) Ann. N.Y. Acad. Sci. 983, 84-100.
- Vigushin, D.M. and Coombes, R.C. (2004) Curr. Cancer Drug Targets 4, 205-218.
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