Pure human recombinant protein
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DPY-30 (human recombinant)

Item No. 11178

Technical Information
Synonyms
  • DPY-30-like protein
  • hDPY-30
  • SAF19
Purity
≥95%
Source
recombinant protein expressed in E. coli
Amino Acids
Amino Acids: 2-99 (full length)
MW
11.2 kDa
50 mM Tris, pH 8.0, 100 mM sodium chloride, and 20% glycerol
License
SUMOpro tag was used under non-exclusive license from LifeSensors, Inc.
UniProt Accession №
Q9C005
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    Product Description

    DPY-30 is a component of the MLL1 methylation complex, which interacts directly with Ash2L.1 In C. elegans, DPY-30 is required for dosage compensation in XX individuals, and its deletion or mutation is lethal. For XO individuals, DPY-30 is required for proper growth and development.2,3 DPY-30 is a homodimer in solution, and two monomers interact with one Ash2L monomer.4 Addition of DPY-30 to the MLL1, WDR5, RbBP5, and Ash2L complex results in a 2-fold increase in methylation rate, from 300x the MLL1 basal rate to 600x the MLL1 basal rate.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. South, P.F., Fingerman, I.M., Mersman, D.P., et alA conserved interaction between the SDI domain of Bre2 and the Dpy-30 domain of Sdc1 is required for histone methylation and gene expression. The Journal of Biological Chemisty 285(1), 595-607 (2010).

    2. Hsu, D.R., and Meyer, B.J. The dpy-30 gene encodes an essential component of the Caenorhabditis elegans dosage compensation machinery. Genetics 137, 999-1018 (1994).

    3. Hsu, D.R., Chuang, P.T., and Meyer, B.J. DPY-30, a nuclear protein essential early in embryogenesis for Caenorhabditis elegans dosage compensation. Development 121(10), 3323-3334 (1995).

    4. Patel, A., Dharmarajan, V., Vought, V.E., et alOn 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).

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