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TP53BP1 tudor-like region (human recombinant)

Item No. 14073

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 53BP1
  • Tumor Suppressor p53-binding Protein 1
Purity
≥90%
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
1717-1972 (N- and C-terminal truncations)
MW
42.6 kDa
Formulation (Request formulation change)
50 mM Tris-HCl, pH 8.0, containing 150 mM sodium chloride and 20% glycerol
UniProt Accession №
Q12888
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $382

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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. They 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 Tudor domains recognize symmetric methylated arginine or methylated lysine residues.4,5,6,7 TP53BP1 binds both histone and non-histone substrates.4,8,9 Binding of TP53BP1 to dimethylated lysine 382 on p53 (p53 K382me2), as well as histone H4K20me2, through the tudor domain, has been shown to be important for TP53BP1 localization to DNA double strand breaks.8,10 This product contains the tudor domain of TP53BP1.

    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. Lasko, P. Tudor domain. Curr. Biol. 20(16), R666-R667 (2010).

    3. 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).

    4. 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).

    5. 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).

    6. 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).

    7. 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).

    8. Kachirskaia, I., Shi, X., Yamaguchi, H., et al. Role for 53BP1 tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling. The Journal of Biological Chemisty 283(50), 34660-34666 (2008).

    9. Stewart, G.S. The demise of a TUDOR under stress opens a chromatin link to 53BP1. EMBO J. 31(8), 1847-1849 (2012).

    10. Zgheib, O., Pataky, K., Brugger, J., et al. An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks. Mol. Cell. Biol. 29(4), 1050-1058 (2009).