Host: E. coli • AA: 1-350 (C-terminal truncation) • Tag: N-terminal His • MW: 43 kDa
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JMJD2A (human, recombinant; His-tagged)

Item No. 10336

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Lysine (K)-specific Demethylase 4A
  • JHDM3A
  • Jumonji Domain Containing 2A
  • KDM4A
Purity
≥95% estimated by SDS-PAGE
Source
Recombinant N-terminal His-tagged protein expressed in E. coli
Amino Acids
1-350 (C-terminal truncation)
MW
43 kDa
Formulation (Request formulation change)
50 mM HEPES, pH 7.4, containing 150 mM sodium chloride and 20% glycerol
Host
E. coli
Applications
ELISA, WB
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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    Cayman Chemical
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    Product Description

    Jumonji Domain Containing 2A (JMJD2A) is a lysine-specific demethylase that catalyzes the demethylation of histone H3 at lysine residues 9 and 36 and histone H1.4 at lysine residue 26.1,2,3 It is composed of the JmjN N-terminal domain, JmjC catalytic domain, two plant homeodomains (PHDs), and two tudor domains that recognize the methylated histones.3 JMJD2A is ubiquitously expressed and localized to the nucleus.4 It is involved in the regulation of gene expression in a context-dependent manner, having roles in both transcriptional silencing and activation of androgen and estrogen receptors (ERs).3 Knockdown of JMJD2A inhibits the proliferation of ER-positive and -negative breast cancer cells and induces apoptosis and cell cycle arrest in colon cancer cells. It is overexpressed in various cancers, including prostate, lung, and colorectal, as well as glioblastomas and endometrial carcinomas, and is associated with higher tumor grade and decreased disease-free survival in breast cancer.5 Cayman's JMJD2A (human, recombinant) can be used for ELISA and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. 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).

    2. Lee, J., Thompson, J.R., Botuyan, M.V., et al. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat. Struct. Mol. Biol. 15(1), 109-111 (2008).

    3. Berry, W.L., and Janknecht, R. KDM4/JMJD2 histone demethylases: Epigenetic regulators in cancer cells. Cancer Res. 73(10), 2936-2942 (2013).

    4. Gray, S.G., Iglesias, A.H., Lizcano, F., et al. Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. The Journal of Biological Chemisty 280(31), 28507-28518 (2005).

    5. Lee, D.H., Kim, G.W., Jeon, Y.H., et al. Advances in histone demethylase KDM4 as cancer therapeutic targets. The FASEB Journal 34(3), 3461-3484 (2020).