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.

IF: Use at a dilution of 1/1000. (Determined by indirect immunofluorescence using the NIH3T3 mouse fibroblast cell line treated with sodium butyrate. WB: Use at a dilution of 1/1000. Detects a band of approximately 17 kDa. (Determined by immunoblotting using a using a whole cell extract of the mouse fibroblast NIH3T3 cell line treated with sodium butyrate.)Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. We advise you to centrifuge this product vial before use.

Type: Primary
Antigen: H3F3A
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Mouse, Rat, Xenopus laevis, Bovine