Cayman JMJD2A (human, recombinant; Strep-tagged)

Methylation of lysine residues of core histones plays a critical role in the regulation of gene expression. Jumonji domain containing 2A (JMJD2A) is the first reported trimethyllysine-specific histone demethylase. It catalyzes the demethylation of trimethylated forms of histone at lysine residues 9 and 36. Like other JmjC protein hydroxylase family members, JMJD2A is an α-ketoglutarate-dependent Fe (II) oxygenase. Purification of Fe-dependent JmjC family members by IMAC can result in displacement of the catalytic iron and decreased activity, therefore this Strep-tagged protein is purified by affinity chromatography using Strep-Tactin coated resin. JMJD2A’s transcriptional function appears to depend on protein associations, as it is implicated in both transcriptional silencing and upregulation of the androgen receptor-dependent genes. Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylases may be drug discovery targets for therapeutic intervention.

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