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Methylation of lysine residues in core histones plays a critical role in regulating gene expression. Jumonji domain containing 2D (JMJD2D) catalyzes the demethylation of di- and tri-methylated forms of histone H3 at lysine residue 9 (me 2/3), leading to transcriptional repression and activation, respectively. Like other JmjC protein hydroxylase family members, JMJD2D 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. Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylase inhibitors may have the capacity to be anticancer agents.
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Technical Information
Synonyms
Jumonji Domain Containing 2D
KDM4D
Lysine-specific Demethylase 4D
Purity
≥70% estimated by SDS-PAGE
Source
active recombinant N-terminal Strep II-tagged protein expressed in E. coli