Active, pure human recombinant enzyme
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Alternative(s)
10335JMJD2D (human, recombinant)
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JMJD2D Strep-tagged (human recombinant)

Item No. 11300

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
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
Amino Acids
4-354
MW
42.6 kDa
Formulation (Request formulation change)
20 mM HEPES, pH 7.4, and 150 mM sodium chloride
License
Sold under license from IBA.
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

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    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 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.4 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).

    4. Krishnan, S., Collazo, E., Ortiz-Tello, P.A., et al. Purification and assay protocols for obtaining highly active Jumonji C demethylases. Anal. Biochem. 420(1), 48-53 (2012).