Active, pure human recombinant enzyme
Related Products
Alternative(s)
11300JMJD2D Strep-tagged (human recombinant)
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JMJD2D (human, recombinant)

Item No. 10335

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • JHDM3D
  • Jumonji Domain Containing 2D
  • KDM4D
  • Lysine-Specific Demethylase 4D
Purity
≥75% estimated by SDS-PAGE
Source
Active human recombinant N-terminal His-tagged protein, expressed in E. coli
MW
42.7 kDa
Formulation (Request formulation change)
A solution in 50 mM HEPES, pH 7.4, with 150 mM sodium chloride and 20% glycerol
UniProt Accession №
Q6B0I6
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    100 µg

    $528

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    Product Description

    Methylation of lysine residues in core histones plays a critical role in regulating gene expression.1 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.2 Like other JmjC protein hydroxylase family members, JMJD2D is an α-ketoglutarate-dependent Fe (II) oxygenase.3 Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylase inhibitors may have the capacity to be anticancer agents.1

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Hamada, S., Kim, T.D., Suzuki, T., et al. Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors. Bioorg. Med. Chem. Lett. 19(10), 2852-2855 (2009).

    2. Kouzarides, T. Chromatin modifications and their function. Cell 128(4), 693-705 (2007).

    3. Couture, J.-F., Collazo, E., Ortiz-Tello, P.A., et al. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nat. Struct. Mol. Biol. 14(8), 689-695 (2007).