Histone H4- along with H2A, H2B, and H3- is involved in the structure of chromatin in eukaryotic cells. Histone H4 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 H4, which results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. In most species, histone H4 is primarily acetylated at lysine 5, 8, 12, and 16.
Rabbit polyclonal antibody raised against a synthetic peptide corresponding to N-terminus of histone H4 acetylated at K12.
Protein A purified
Detects histone H4 only when acetylated at K12 in mouse, rat, and human
PBS (pH 7.5), 0.1% gelatin
4°C, stable for 1 year from the date of shipment. Avoid repeated freezing and thawing. Multiple freeze/thaw cycles may result in decreased performance
H4K12ac antibody, H4K12a antibody
WB: 1:200-1:1000, IF: 1:100-1:500, IHC: 1:100-1:500, ELISA: 1:1000-1:2000, IP: 2 μg/106 cells
Fig. 1. WB analysis of Histone H4K12ac (Acetyl H4K12) Polyclonal Antibody with NIH-3T3 cell lysates (A-4029).