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 alpha-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.Synonyms: JHDM3A, Jumonji Domain Containing 2A, KDM4A, Lysine (K)-specific Demethylase 4A. Purity: >95% estimated by SDS-PAGE. Source: Recombinant N-terminal Strep II-tagged protein expressed in E. coli. Amino Acids: 2-350. MW: 42.7 kDa. Formulation: (Request formulation change), 20 mM HEPES, pH 7.4, and 150 mM NaCl. License: Sold under license from IBA.. UniProt Accession #: O75164.