epitope corresponding to phosphorylated Ser 39 of HDAC8 of human origin
Modification
Phosphoralated
Modification Notes
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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IFIHC
recommended for detection of Ser 39 phosphorylated HDAC8 of mouse, rat and human origin by IF and IHC(P):
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Ser 39 of HDAC8 of human origin
Tissue Specificity
epitope corresponding to phosphorylated Ser 39 of HDAC8 of human origin