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Histone Deacetylase 2 (HDAC2) antibody
| Antigen | Histone Deacetylase 2 (HDAC2) |
| Synonyms | RPD3, YAF1, Yy1bp, mRPD3, D10Wsu179e |
| Clonality | Polyclonal |
| Host |
Alternatives Rabbit |
| Reactivity |
Alternatives Chicken |
| Conjugate |
Alternatives Un-conjugated |
| Application |
Alternatives Chromatin Immunoprecipitation (ChiP), Dot Blot (Dot), Immunoprecipitation (IP), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB) |
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11 references available |
| Catalog no. | ABIN150633 |
| Quantity | 50 µl (12.4 mg/ml) |
| Price | Product not available in this region. |
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Additional Information
| Alternative name | HDAC2 |
| Immunogen | Synthetic peptide: C-SGEKTDTKGTKSEQLSNP conjugated to KLH, corresponding to amino acids 471-488 of Human HDAC 2. |
| Cross-Reactivity | Chicken, Human, Mouse (Murine), Rat (Rattus) |
| Isotype | IgG |
| Description | Reversible acetylation of highly conserved lysine residues in N-terminal tail domains of core histones plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs) (Taunton et al.). Histone deacetylases activities were often, but not always, associated with transcriptional repression and nucleosomal condensations (Wolffe 1996 and Grunstein 1997). |
| Specificity | Anti-Histone Deacetylase 2 specifically recognizes histone deacetylase 2 by immunoblotting and immunoprecipitation (55 kD). The sequence recognized by the antibody is highly conserved in mouse and chicken. |
Application Details
| Application Notes | ChIP: Use 2ul for 10^6 cells. Dot: Use at an assay dependent dilution. IHC-P: Use at a dilution of 1/500. Perform enzymatic antigen retrieval before commencing with IHC staining protocol. IP: Use at a dilution of 1/2500. WB: Use at a dilution of 1/2000-1/20000. Predicted molecular weight: 55.3 kDa. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. |
| Concentration | 12.4 mg/ml |
| Purification | Purified IgG fraction |
| Buffer | 0.01M PBS pH7.4 |
| Preservative | 15mM Na azide |
| Storage | Store at 4 C. Aliquot and store at -20 C long-term. |
| Research Area | Cardiovascular, Hypertrophy, DNA/RNA, Transcription Factors, Wnt Signaling |
| Restrictions | For Research Use only |
Publications
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Bauer, Hayes, White et al.: "Nucleosome structural changes due to acetylation." in: Journal of molecular biology, Vol. 236, Issue 3, pp. 685-90, 1994 (PubMed).
Lee, Hayes, Pruss et al.: "A positive role for histone acetylation in transcription factor access to nucleosomal DNA." in: Cell, Vol. 72, Issue 1, pp. 73-84, 1993 (PubMed). Wolffe: "Histone deacetylase: a regulator of transcription." in: Science (New York, N.Y.), Vol. 272, Issue 5260, pp. 371-2, 1996 (PubMed). Taunton, Hassig, Schreiber: "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p." in: Science (New York, N.Y.), Vol. 272, Issue 5260, pp. 408-11, 1996 (PubMed). Grunstein: "Histone acetylation in chromatin structure and transcription." in: Nature, Vol. 389, Issue 6649, pp. 349-52, 1997 (PubMed). Lin, Nagy, Inoue et al.: "Role of the histone deacetylase complex in acute promyelocytic leukaemia." in: Nature, Vol. 391, Issue 6669, pp. 811-4, 1998 (PubMed). Hassig, Tong, Fleischer et al.: "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 7, pp. 3519-24, 1998 (PubMed). Zhang, LeRoy, Seelig et al.: "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities." in: Cell, Vol. 95, Issue 2, pp. 279-89, 1998 (PubMed). Tong, Hassig, Schnitzler et al.: "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex." in: Nature, Vol. 395, Issue 6705, pp. 917-21, 1998 (PubMed). Fischle, Emiliani, Hendzel et al.: "A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p." in: The Journal of biological chemistry, Vol. 274, Issue 17, pp. 11713-20, 1999 (PubMed). Grozinger, Hassig, Schreiber: "Three proteins define a class of human histone deacetylases related to yeast Hda1p." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 9, pp. 4868-73, 1999 (PubMed). |
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Alternatives
Alternatives for antigen "Histone Deacetylase 2 (HDAC2)", type "Antibodies"




Alternatives