Histone H3 along with H2A, H2B and H4 is involved in the structure of chromatin in eukaryotic cells. Histone H3 can undergo several different types of epigenetic modifications that influence cellular processes. These modifications, including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation, occur on the N-terminal tail domains of histone H3, which results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23.
Rabbit polyclonal antibody raised against a synthetic peptide corresponding to the N-terminus of histone H3 acetylated on K23, ChIP-grade
Protein A purified
Detects histone H3 only when acetylated at K23 in mouse, rat, and human
PBS (pH 7.5), 150 mM NaCl, 50% glycerol
-20°C, stable for 1 year from the date of shipment. Avoid repeated freezing and thawing. Multiple freeze/thaw cycles may result in decreased performance
H3K23ac antibody, H3K23a antibody
WB: 1:200-1:1000, IHC: 1:100-1:500, ELISA: 1:1000-1:2000 IP: 2 μg/106 cells
Fig. 1. WB analysis of Histone H3K23ac (Acetyl H3K23) Polyclonal Antibody with sodium butyrate-induced Hela cell lysates (A-4025).