Anti-dimethyl Histone H3 (Arg2) Antibody

Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm. The most commonly studied modifications are acetylation, phosphorylation, methylation, and ubiquitination. These modifications can alter local chromatin architecture, or recruit trans-acting factors that recognize specific histone modifications (the "histone code" hypothesis). The modifications occur predominantly on the N-terminal and C-terminal tails that extend beyond the nucleosome core particle. Histone H3 Arg2 methylation is a widespread silencing modification that inhibits histone H3 Lys4 trimethylation.

Broad species reactivity is expected.

This antibody recognizes the N-terminus of Histone H3 dimethylated at Arg2.

KLH-conjugated linear peptide corresponding to the N-terminus of human Histone H3 dimethylated at Arg2.

Detect Histone H3 using this rabbit polyclonal antibody, Anti-dimethyl Histone H3 (Arg2) Antibody validated for use in western blotting & Dot Blot.

Western Blotting Analysis: A 1:620 dilution of this antibody detected dimethyl Histone H3 (Arg2) in CARM1 treated dimethyl Histone H3 (Arg2) recombinant protein, but demonstrated a loss of signal in untreated dimethyl Histone H3 (Arg2) recombinant protein. (Note: CARM1 is a methyl transferase that results in the methylation of Histone H3.).

Dot Blot (Specificity) Analysis: A 1:620 dilution from a representative lot detected dimethyl Histone H3 (Arg2) peptides, but not unmethylated Histone H3 (Arg2) or other peptides corresponding to modified histones.

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Evaluated by Western Blotting in HeLa acid extract.

Western Blotting Analysis: A 1:620 dilution from a representative lot detected dimethyl Histone H3 (Arg2) in 10 µg of HeLa acid extract.

~17 kDa observed. Uncharacterized band(s) may be observed in some cell lysates.