Tudor domains are small protein structural motifs of about ~50aa related to the “royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains. Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling. The tudor domains recognize symmetric methylated arginine or methylated lysine residues. JMJD2A catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3). However, the tudor domain of this protein has been shown to bind histone H3K4me, H3K9me3, and H3K20me2/3. Like other JmjC protein hydroxylase family members, JMJD2A is an alpha-ketoglutarate-dependent Fe (II) oxygenase. This product contains the tandem tudor domains of JMJD2A.||Source:|Recombinant protein corresponding to aa888-1023 from the tandem tudor domains of human JMJD2A, fused to GST-tag at N-terminal, expressed in E. coli. ||Molecular Weight: |~42.2kD (aa888-1023, NT GST-tag)||Storage and Stability:|Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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