JMJD6 also known as bifunctional arginine demethylase and lysyl-hydroxylase JMJD6. JMJD6 acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as u2AF2/u2AF65 and LuC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of u2AF2/u2AF65, affecting the pre-mRNA splicing activity of u2AF2/u2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. Recombinant human JMJD6, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.