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L3MBTL1 MBT domains (human recombinant; GST-tagged)

Item No. 14775

Technical Information
Synonyms
  • H-l(3)MBT
  • Lethal(3)Malignant Brain Tumor-like Protein 1
  • L(3)MBT-like
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
191-350
MW
65.5 kDa
50 mM Tris, pH 8.0, with 150 mM sodium chloride and 20% glycerol
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    The malignant brain tumor (MBT) domain is structurally related to chromatin binding domains, such as chromodomains, tudor domains, and PWWP-domains.1,2 MBT domain-containing proteins have a variable number of MBT repeats. The MBT domains recognize methylated lysines on histone tails with varying degree of specificity for the various methyl marks.1 L3MBTL1, a human homolog of the Drosophila lethal(3)MBT protein, is a member of the polycomb group (PcG) of proteins that functions as a transcriptional repressor.3 L3MBTL1 contains three MBT repeat domains which collectively bind to either histone H3 or H4.1,4 The second and third MBT domains were found to bind preferentially to mono- and dimethylated lysines of histone H3 at lysine 4 (H3K4me1) and histone H4 at lysine 20 (H4K20me2).4,5 Recognition of methyl-lysine marks by MBT domains leads to chromatin compaction and a repressed transcriptional state.4,6 Further, L3MBTL1 has a tumor suppressor function and is thought to play a role in maintaining genomic stability and DNA replication.7,8 This protein product contains the MBT repeat region of L3MBTL1.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Trojer, P., and Reinberg, D. Beyond histone methyl-lysine binding: How malignant brain tumor (MBT) protein L3MBTL1 impacts chromatin structure. Cell Cycle 7(5), 578-585 (2008).

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

    3. Boccuni, P., MacGrogan, D., Scandura, J.M., et alThe human L(3)MBT polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6). The Journal of Biological Chemisty 278(17), 15412-15420 (2003).

    4. Trojer, P., Li, G., Sims, R.J., III, et alL3MBTL1, a histone-methylation-dependent chromatin lock. Cell 129(5), 915-928 (2007).

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

    6. Kalakonda, N., Fischle, W., Boccuni, P., et alHistone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1. Oncogene 27(31), 4293-4304 (2008).

    7. Acs, K., Luijsterburg, M.S., Ackermann, L., et alThe AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18(12), 1345-1350 (2011).

    8. Gurvich, N., Perna, F., Farina, A., et alL3MBTL1 polycomb protein, a candidate tumor suppressor in del(20q12) myeloid disorders, is essential for genome stability. Proc. Natl. Acad. Sci. USA 107(52), 22552-22557 (2010).