Background:

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, PCAF (for p300/CBP-associated factor), p300/CBP and the TFIID subunit TAF II p250. Mammalian HDAC7 is a histone deacetylase that interacts with the adaptor mSin3A. The interaction of HDAC7 with mSin3A suggests the association of multiple repression complexes of transcription factors.

Specificity:

Histone Deacetylase 7 (Phospho-S155) polyclonal antibody detects endogenous levels of Histone Deacetylase 7 protein only when phosphorylated at Ser155.

Alternative names:

Histone deacetylase 7; HDAC 7; HDAC-7

Species reactivity:

Human,Mouse,Rat

Host:

Rabbit

Ig type:

Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Immunogen:

Synthetic phosphopeptide derived from human Histone Deacetylase 7 around the phosphorylation site of Serine 155.

Purification & Purity:

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Molecular weight:

~ 105 kDa

Applications:

WB IF

Usage:

WB: 1:500~1:1000 IHC: 1:50~1:200

Storage:

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

More info:

Email: info@sobekbio.com

Orders:

Email: orders@sobekbio.com