Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

WB: Use at a concentration of 1 - 2 ?g/ml. Detects a band of approximately 17 kDa. (Determined using a whole cell extract of mouse fibroblasts 3T3 cell line treated with sodium butyrate.)Indirect ELISA: Use at an assay dependent dilution. ICC: Use at an assay dependent dilution. Not tested in other applications. Optimal dilutions/concentrations should be determined by the researcher. We advise you to centrifuge this product vial before use.

Type: Primary
Antigen: H3F3A
Clonality: Monoclonal
Clone: AH3-120
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG1
Reactivity: Human, Mouse, Drosophila, Rat