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RbBP5 (human, recombinant)

Item No. 10947

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • RBQ3
  • Retinoblastoma binding Protein 5
  • SWD1, Set1c WD40 repeat protein, homolog
Purity
≥80%
Source
Recombinant protein expressed in E. coli
Amino Acids
2-538 (full length)
MW
72.9 kDa
Formulation (Request formulation change)
50 mM Tris, pH 8.0, containing 150 mM sodium chloride and 20% glycerol
License
SUMOpro tag was used under non-exclusive license from LifeSensors, Inc.
UniProt Accession №
Q15291
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.

    50 µg

    $456

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    Product Description

    Retinoblastoma-binding protein 5 (RbBP5) is a ubiquitously expressed nuclear protein that contains WD40 repeat-like domains. RbBP5 binds directly to tumor suppressor retinoblastoma protein (RB) and regulates cell proliferation. Interaction of RbBP5 occurs preferentially with underphosphorylated RB through the E1A-binding pocket B.1 RbBP5 is also an important component of the multi-subunit SET1 lysine methyltransferase protein complex, which includes MLL1.2 RbBP5 interacts directly with WDR5 contributing to the activation of the MLL1 core protein complex.3,4,5 MLL1-4 protein complexes catalyze the di- and trimethylation of histone H3 at lysine 4 (H3K4me2/me3), leading to the maintenance of global H3K4 trimethylation.6

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Sugano, M., Tsuchida, K., and Makino, N. Nifedipine prevents apoptosis of endothelial cells induced by oxidized low-density lipoproteins. J. Biomed. Sci. 40(1), 146-152 (2002).

    2. Steward, M.M., Lee, J.S., O'Donovan, A., et al. Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes. Nat. Struct. Mol. Biol. 13(9), 852-854 (2009).

    3. Avdic, V., Zhang, P., Lanouette, S., et al. Structural and biochemical insights into MLL1 core complex assembly. Structure 19(1), 101-108 (2011).

    4. Odho, Z., Southall, S.M., and Wilson, J.R. Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1. The Journal of Biological Chemisty 285(43), 32967-32976 (2010).

    5. Dou, Y., Milne, T.A., Ruthenburg, A.J., et al. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nat. Struct. Mol. Biol. 13(8), 713-719 (2006).

    6. Wang, P., Lin, C., Smith, E.R., et al. Global analysis of H3K4 methylation defines MLL family member targets and points to a role for MLL1-mediated H3K4 methylation in the regulation of transcriptional initiation by RNA polymerase II. Mol. Cell Biol. 29(22), 6074-6085 (2009).