Histone Deacetylase 4 (HDAC4) (pSer246) antibody

Details for Product No. ABIN362451
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Antigen
Synonyms
CG1770, DHDAC4, Dmel\\CG1770, GC1770, HDAC, HDAC4a, dHDAC4, dmHDA405, hdac4, dana_GLEANR_19966, DanaGF18710, GF18710, HDAC4, AHO3, BDMR, HA6116, HD4, HDAC-4, HDAC-A, HDACA, 4932408F19Rik, AI047285, wu ... show more
CG1770, DHDAC4, Dmel\\CG1770, GC1770, HDAC, HDAC4a, dHDAC4, dmHDA405, hdac4, dana_GLEANR_19966, DanaGF18710, GF18710, HDAC4, AHO3, BDMR, HA6116, HD4, HDAC-4, HDAC-A, HDACA, 4932408F19Rik, AI047285, wu:fa96d08, wu:fc56f08, zgc:152701 show less
Epitope
pSer246
(38), (28), (15), (9), (7), (7), (6), (4), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human, Mouse (Murine)
(186), (95), (76), (31), (24), (24), (1), (1), (1), (1)
Host
Rabbit
(170), (20), (2)
Clonality
Polyclonal
Conjugate
Un-conjugated
(6), (6), (6), (3), (3), (3), (3), (3), (3), (3), (3), (2), (2), (2)
Application
Western Blotting (WB), Immunohistochemistry (IHC)
(163), (58), (30), (28), (26), (22), (14), (11), (6), (3), (1)
Pubmed 4 references available
Quantity 50 µL
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Catalog No. ABIN362451
198.00 $
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Immunogen Peptide sequence around phosphorylation site of pSer246, 259, 220 (T-A-S (p) -EP) derived from Human HDAC4, HDAC5, HDAC9. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
Isotype IgG
Specificity The antibody detects endogenous level of HDAC4/HDAC5/HDAC9 only when phosphorylated at serine 246/259/220.
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Alternative Name HDAC4/HDAC5/HDAC9
Background Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general,they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs, classes 1, 2 and 4, which are closely related Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is effected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.
Molecular Weight 124 kDa
NCBI Accession NP_055522, NP_001015
UniProt Q9UKV0
Application Notes Western blotting: 1:500-1:1000
Immunohistochemistry: 1:50-1:100
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Store at -20 °C for long term preservation (recommended). Store at 4 °C for short term use.
Background publications Cress, Seto: "Histone deacetylases, transcriptional control, and cancer." in: Journal of cellular physiology, Vol. 184, Issue 1, pp. 1-16, 2000 (PubMed).

Marmorstein: "Structure and function of histone acetyltransferases." in: Cellular and molecular life sciences : CMLS, Vol. 58, Issue 5-6, pp. 693-703, 2001 (PubMed).

Thiagalingam, Cheng, Lee et al.: "Histone deacetylases: unique players in shaping the epigenetic histone code." in: Annals of the New York Academy of Sciences, Vol. 983, pp. 84-100, 2003 (PubMed).

Vigushin, Coombes: "Targeted histone deacetylase inhibition for cancer therapy." in: Current cancer drug targets, Vol. 4, Issue 2, pp. 205-18, 2004 (PubMed).

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