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Phospho-HDAC8 (Ser39) Rabbit anti-Human, Polyclonal, Bioss
SDP

Catalog No. 501985161
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50-198-5161 100 μL
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Catalog No. 50-198-5161 Supplier Bioss Supplier No. BS3127R
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Rabbit Polyclonal Antibody

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 (p300/CBP-associated factor), p300/CBP, HAT1 and the TFIID subunit TAF II p250. Mammalian HDAC8, isolated from human kidney, is a histone deacetylase that shares homology to other HDACs but has different tissue distribution. HDAC8 is localized to the nucleus and plays a role in the development of a broad range of tissues and in the etiology of cancer.

Specifications

Antigen Phospho-HDAC8 (Ser39)
Applications Immunofluorescence, Immunohistochemistry (Paraffin), Western Blot
Classification Polyclonal
Concentration 1 μg/mL
Conjugate Unconjugated
Formulation PBS with 1% BSA, 50% glycerol and 0.09% sodium azide; pH
Gene HDAC8
Gene Accession No. Q9BY41
Gene Alias 2610007D20Rik; CDA07; CDLS5; HD8; HDAC8; HDACL1; Histone deacetylase 8; histone deacetylase-like 1; MRXS6; RGD1562895; RPD3; WTS
Gene Symbols HDAC8
Host Species Rabbit
Immunogen KLH conjugated synthetic phosphopeptide derived from human HDAC8 around the phosphorylation site of Ser39.
Purification Method Protein A
Quantity 100 μL
Regulatory Status RUO
Primary or Secondary Primary
Gene ID (Entrez) 55869
Target Species Human
Content And Storage -20°C
Product Type Antibody
Form Liquid
Isotype IgG
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