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JMJD2C tudor domain (human, recombinant)

Item No. 9001953

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • GASC-1 Protein
  • KDM4C
  • Lysine-specific Demethylase 4C
  • JmjC Domain-containing Histone Demethylation Protein 3C
  • Jumonji Domain-containing Protein 2C
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
869-1,003 (tudor domain)
MW
39.89 kDa
Formulation (Request formulation change)
50 mM Tris, pH 7.5, containing 150 mM sodium chloride and 20% glycerol
UniProt Accession №
Q9H3R0
Origin
Animal/Rabbit
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $662

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    Product Description

    Tudor domains are small protein structural motifs of ~50 amino acids related to the “royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains.1,2 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.3 The tudor domains recognize symmetric methylated arginine or methylated lysine residues.4,5,6,7 JMJD2C is an α-ketoglutarate-dependent Fe (II) oxygenase that catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3).8 This protein product contains the tandem tudor domains of JMJD2C.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Maurer-Stroh, S., Dickens, N.J., Hughes-Davies, L., et al. The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends Biochem. Sci. 28(2), 69-74 (2003).

    2. Chen, C., Nott, T.J., Jin, J., et al. Deciphering arginine methylation: Tudor tells the tale. Nat. Rev. Mol. Cell Biol. 12(10), 629-642 (2011).

    3. Kim, J., Daniel, J., Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 7(4), 397-403 (2006).

    4. Huang, Y., Fang, J., Bedford, M.T., et al. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312(5774), 748-751 (2006).

    5. 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).

    6. Sprangers, R., Groves, M.R., Sinning, I., et al. High-resolution X-ray and NMR structures of the SMN tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol. 327(2), 507-520 (2003).

    7. Pedersen, M.T., Agger, K., Laugesen, A., et al. The demethylase JMJD2C localizes to H3K4me3-positive transcription start sites and is dispensable for embryonic development. Mol. Cell. Biol. 34(6), 1031-1045 (2014).