Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).
Rabbit polyclonal antibody raised against a synthetic peptide corresponding to the monomethylated histone H3 at K27, ChIP-grade
Broad Range, Mouse, Rat, Human
A synthetic methylated peptide corresponding to residues surrounding K27 of human histone H3
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3
Store at -20°C (regular) or -80°C (long term). Avoid freeze / thaw cycles.
H3K27me1 antibody, H3K27m1 antibody, HIST1H3J, H3/j, H3FJ, Histone H3.1, Histone H3/a, Histone H3/b, Histone H3/c, Histone H3/d, Histone H3/f, Histone H3/h, Histone H3/I, Histone H3/j, Histone H3/k, Histone H3/l, HIST3H3
WB 1:500 - 1:2000
IHC 1:50 - 1:200
IF 1:50 - 1:200
IP 1:50 - 1:200
ChIP 1:20 - 1:100