Histone Deacetylase 3 (HDAC3) (AA 2-17) antibody

Details for Product No. ABIN151195
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Synonyms CG2128, DHDAC3, DmHDAC3, Dmel\\CG2128, Dromel_CG2128_FBtr0078767_hdac3_mORF, HDAC, HDAC3, Hdac 3, dHDAC3, dmHDA402, hdac3, HDm, hd3, RPD3, XRpd3, rpd3-2, HD3, RPD3-2, AW537363, zgc:55927
AA 2-17
(31), (23), (17), (7), (5), (4), (3), (3), (3), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
(169), (76), (73), (2), (1), (1), (1), (1), (1)
(132), (39)
(3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Western Blotting (WB), Chromatin Immunoprecipitation (ChIP), Immunohistochemistry (IHC), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunoprecipitation (IP)
(144), (73), (62), (53), (33), (22), (20), (17), (6), (6), (3), (3), (1), (1)
Pubmed 3 references available
Quantity 0.1 mg
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Catalog No. ABIN151195
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Immunogen This antibody was generated by immunizing rabbits with a synthetic peptide corresponding to amino acids 2-17 of human HDAC3.
Specificity In HeLa, a 50 kDa band is observed.
Cross-Reactivity (Details) Expected to cross-react with Mouse (100% identity with immunogen), rat,(100% identity with immunogen),Chicken (100% identity with immunogen) due to sequence homology. Not yet tested in other species.
Purification Protein G purified
Alternative Name HDAC3
Background Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes thatregulate transcription by selectively deacetylating or acetylating the eta-amino groups oflysines located near the amino termini of core histone proteins (1). Eight members ofHDAC family have been identified in the past several years (2,3). These HDAC familymembers are divided into two classes, I and II. Class I of the HDAC family comprisesfour members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domainexhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC familycomprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofoldlarger than those of the class I members, and the deacetylase domains are presentwithin the C-terminal regions, except that HDAC-6 contains two copies of the domain,one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showedtissue-specific expression patterns (3). These results suggested that each member ofthe HDAC family exhibits a different, individual substrate specificity and function in vivo. Alternate Names: anti-HD3 antibody, anti-RPD3 antibody, anti-RPD3-2 antibody.
Gene Symbol: HDAC3
Gene ID 8841
Research Area Cancer, Hypertrophy, DNA/RNA, Transcription Factors
Application Notes In HeLa, a 50 kDa band is observed.
Recommended dilutions: Chromatin Immunoprecipitation 1:10-1:500, Immunohistochemistry 1:10-1:2000, Immunohistochemistry-Paraffin 1:10-1:2000, Immunoprecipitation 1:10-1:500, Western Blot 2 - 5µg/mL
Restrictions For Research Use only
Concentration 0.5 mg/mL
Buffer PBS containing 0.05 % BSA, Sodium Azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Handling Advice Avoid freeze-thaw cycles
Storage 4 °C
Storage Comment 4 °C short term. Aliquot and store at -20 °C long term.
Supplier Images
anti-Histone Deacetylase 3 (HDAC3) (AA 2-17) antibody anti-Histone Deacetylase 3 (HDAC3) (AA 2-17) antibody
General Wilson, Byun, Nasser et al.: "HDAC4 promotes growth of colon cancer cells via repression of p21." in: Molecular biology of the cell, Vol. 19, Issue 10, pp. 4062-75, 2008 (PubMed).

Nakayama, Takami: "Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure." in: Journal of biochemistry, Vol. 129, Issue 4, pp. 491-9, 2001 (PubMed).

Cress, Seto: "Histone deacetylases, transcriptional control, and cancer." in: Journal of cellular physiology, Vol. 184, Issue 1, pp. 1-16, 2000 (PubMed).

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