Host: E. coli • AA: 3,762-3,969 (N-terminal truncations) • Tag: N-terminal His and SUMOpro tag • MW: 24.1 kDa
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Product Categories

Product Type

Proteins

Research Area

Epigenetics, Transcription, & Translation
Writers
Histone Methylation

Application

MLL1 (human recombinant)

Item No. 10658

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • ALL1
  • CXXC-type zinc finger protein 7
  • HRX
  • KMT2a
  • Lysine Methyltransferase 2A
  • Mixed Lineage Leukemia 1
Purity
≥80% estimated by SDS-PAGE
Source
Recombinant protein expressed in E. coli
Amino Acids
3,762-3,969 (N-terminal truncation)
MW
24.1 kDa
Formulation (Request formulation change)
50 mM Tris, pH 8.0, with 400 mM sodium chloride, 10% glycerol, and 5 mM 2-mercaptoethanol
License
SUMOpro tag was used under non-exclusive license from LifeSensors, Inc.
UniProt Accession №
Q03164
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $380

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    Product Description

    Mixed Lineage Leukemia (MLL1) plays a major role in epigenetic regulation through methylation of histone 3 at lysine 4 (H3K4) to activate gene transcription. Methylation of H3K4 leads to upregulation of developmental genes, including HOX family members.1 In addition to its methylation activity, MLL1 has been shown to co-localize with Pol II at several genomic elements.2 Consequently, MLL1 has very low basal methyltransferase activity unless complexed with the activating protein complex of WDR5, Ash2L, and RbBP5 (MLL/WAR complex).3 This C-terminal fragment of MLL1, residues 3762 - 3969, contains the SET1 domain for methyltransferase activity, and the WIN motif for binding the WAR complex. The protein DPY-30 has also been reported to associate with the MLL1-WAR complex. MLL1 is also available as a component of the MLL1/WAR complex (Item No. 10756) and MLL1/WARD complex.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Patel, A., Dharmarajan, V., Vought, V.E., et al. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. The Journal of Biological Chemisty 284(36), 24242-24256 (2009).

    2. Mohan, M., Lin, C., Guest, E., et al. Licensed to elongate: A molecular mechanism for MLL-based leukaemogenesis. Nat. Rev. Cancer 10(10), 721-728 (2010).

    3. Smith, E., Lin, C., and Shilatifard, A. The super elongation complex (SEC) and MLL in development and disease. Genes Dev. 25(7), 661-672 (2011).