Methylation of lysine residues of core histones plays a critical role in the regulation of gene expression.1 Jumonji domain containing 2A (JMJD2A) is the first reported trimethyllysine-specific histone demethylase.2 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 -ketoglutarate-dependent Fe (II) oxygenase.3 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.4 JMJD2As transcriptional function appEArs to depend on protein associations, as it is implicated in both transcriptional silencing and upregulation of the androgen receptor-dependent genes.2 Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylases may be drug discovery targets for therapeutic intervention.1Technical InformationSynonymsJHDM3AJumonji Domain Containing 2AKDM4APurity95% estimated by SDS-PAGESourceactive recombinant N-terminal Strep II-tagged protein expressed in E. coliMW42.7 kDaFormulation20 mM HEPES, pH 7.4, and 150 mM sodium chlorideLicenseSold under license from IBA.UniProt Accession O75164