Synthetic phosphopeptide derived from human HDAC4 around the phosphorylation site of Serine 632.
Conjugation:
Unconjugated
Alternative Names:
Histone deacetylase 4, HD4, HDAC4, KIAA0288
In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin. The remodeling of chromatin is believed to be a critical component of transcriptional regulation, and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino-terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Several mammalian proteins have been identified as nuclear histone acetylases, including GCN5, p300/CBP, PCAF (p300/CBPassociated factor), HAT1 and the TFIID subunit TAF II p250. Mammalian HDAC1 (also designated HD1), HDAC2 (also designated RPD3) and HDAC3-6 have been identified as histone deacetylases.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
p-HDAC4 (S632) polyclonal antibody detects endogenous levels of HDAC4 protein only when phosphorylated at Ser632.
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