Anti-methyl-Histone H3 (Me-Lys⁴) antibody produced in rabbit

Histones are proteins that form the nucleosome along with DNA. A nucleosome consists of core histone octamers made of two heterodimers of H2A and H2B along with two heterodimers of H3 and H4. This octamer is bound by the DNA and H1 protein. The HIST3H3 gene is mapped on the human chromosome at 1q42.13.

synthetic methylated peptide corresponding to amino acid 1-8 (Me-Lys⁴) at the N-terminus of human histone H3, conjugated to KLH. The sequence is identical in many species.

Anti-methyl-Histone H3 (Me-Lys4) antibody produced in rabbit detection of [Me-Lys4] histone H3 by immunoblotting, chromatin immunoprecipitation and immunoprecipitation.

Anti-methyl-Histone H3 [Me-Lys4] recognizes histone H3 methylated on Lys4.

Histone methylation like acetylation is a complex dynamic process involved in several processes including transcriptional regulation, chromatin condensation, mitosis, and heterochromatin assembly. Histones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells. Lysine residues can be mono-, di-, and trimethylated at different heterochromatic subdomains adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N- terminal tail domains of histone H3 (Lys4, Lys9, and Lys27) are the preferred sites of methylation. Histone H3 mono-, di-, and trimethylation at Lys4 and Lys9 are carried out both in vitro and in vivo by SET domain site-specific histone methyltransferases (HMTases), including Suv39h1, Suv39h2, and G9a. Di- and trimethylation of histone H3 at Lys4 in coding regions correlates with transcriptional activity of many genes. Dimethylation of Histone H3 at Lys4 occurs at both active and inactive euchromatic regions, but not in silent heterochromatic sites, whereas trimethylation at Lys4 is present exclusively at active genes.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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