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 amino terminus of histone H3 acetylated on K9/14, ChIP-grade
Protein A purified
Detects histone H3 only when acetylated at K9/14 in mouse, rat, and human
10 mM HEPES (pH 7.5), 150 mM NaCl, and 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
H3(K9/14)ac antibody, H3(K9/14)a antibody, H3K9/14ac antibody
WB: 1:200-1:1000, IF: 1:100-1: 500, IH: 1:100-1:500, ELISA: 1:1000-1:2000, IP: 2 μg/106 cells