HDAC 9 (P1047) polyclonal antibody

Q9UKV0

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. Several mammalian proteins function as nuclear histone acetylases, including GCN5, PCAF (p300/CBP-associated factor), p300/CBP, HAT1 and the TFIID subunit TAF II p250. Conversely, the deacetylation of histones is associated with transcriptional silencing. The histone deacetylases (HDAC) include HDAC1-9. HDAC9 and HDAC9a are two alternatively spliced isoforms of HDAC9. HDAC9a is 132 amino acids shorter than HDAC9, but both isoforms contain the HDAC catalytic domain, remain capable of deacetylase activity and repress myoctye enhancer-binding factor 2-mediated transcription.

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

HDAC9 (P1047) pAb detects endogenous levels of HDAC9 protein.

Immunohistochemistry (IHC) analyzes of HDAC 9 (P1047) pAb in paraffin-embedded human breast carcinoma tissue at 1:100.

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

Synthetic peptide, corresponding to the C-terminual of Human HDAC 9.