Pure human recombinant enzyme
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Alternative(s)
10336JMJD2A (human, recombinant; His-tagged)
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JMJD2A (human, recombinant; Strep-tagged)

Item No. 11299

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
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
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $528

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    Product Description

    Methylation of lysine residues of core histones plays a critical role in the regulation of gene expression.1 Jumonji domain containing 2A (JMJD2A) is the first reported trimethyllysine-specific histone demethylase.2 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 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 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.2 Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylases may be drug discovery targets for therapeutic intervention.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. Marmorstein, R., and Trievel, R.C. Histone modifying enzymes: Structures, mechanisms, and specificities. Biochim. Biophys. Acta 1789(1), 58-68 (2009).

    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).