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 phosphorylated at serine 10, serine 28, threonine 3 and threonine11.
Rabbit polyclonal antibody raised against a synthetic peptide corresponding to the phosphorylated histone H3 at Thr11
Protein A purified
Detects histone H3 only when phosphorylated at Thr11 in mouse, rat, and human. Broad species cross-reactivity predicted based on sequence homology
PBS (pH 7.5), 150 mM NaCl, 30% glycerol
Store at -20°C. Avoid repeated freezing and thawing. Multiple freeze/thaw cycles may result in decreased performance
WB: 1:1000-1:2000, IF: 1:100-1:500, IHC: 1:100-1:500, ELISA: 1:1000-1:2000, IP: 2 μg/106 cells