Render Target: SSR
Render Timestamp: 2024-12-19T21:10:36.503Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-29 19:55:26.772
Product last modified at: 2024-12-17T18:59:38.954Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

DDB-1 (D4C8) Rabbit mAb #6998

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 127
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    DDB-1 (D4C8) Rabbit mAb recognizes endogenous levels of total DDB-1 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Chicken, Bovine

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly832 of human DDB-1 protein.

    Background

    Damaged DNA-Binding Protein (DDB) consists of a 127 kDa subunit (DDB-1) and a 48 kDa subunit (DDB-2) that contribute to the formation of the UV-damaged DNA-binding protein complex (UV-DDB) (1-3). In conjunction with CUL4A and ROC-1, the UV-DDB complex forms an E3 ubiquitin ligase that recognizes a broad spectrum of DNA lesions such as cyclobutane pyrimidine dimers, 6-4 photoproducts, apurinic sites and short mismatches. The complex polyubiquitinates components of the nucleotide excision repair pathway (4-6). Loss of DDB activity has been identified in a subset of xeroderma pigmentosum complementation group E (XP-E) patients and has been linked to the deficient repair of cyclobutane pyrimidine dimers in cells derived from these patients (7-10).
    DDB-1 is a relatively abundant protein that is vital for normal cell function and is evolutionarily conserved in mammals, insects, worms and plants. Unlike DDB-2, lesions in DDB-1 have yet to be indentified in XP-E patients. In association with ROC-1 and CUL4A, DDB-1 functions to recruit substrate-specific targeting subunits, generally known as DCAFs or CDWs, to CUL4-RING E3 ubiquitin-protein ligase complexes (11,12). Ubiquitination of histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage by the DDB1-DDB2-CUL4A-ROC1 E3 ubiquitin-protein ligase complex may facilitate their removal from the nucleosome in order to promote DNA repair (13-15). DDB-1, in association with other CUL4-based E3 ligase complexes, has also been found to be a regulator of mTOR signaling (16,17).
    1. Reardon, J.T. et al. (1993) J Biol Chem 268, 21301-8.
    2. Keeney, S. et al. (1993) J Biol Chem 268, 21293-300.
    3. Hwang, B.J. and Chu, G. (1993) Biochemistry 32, 1657-66.
    4. Chu, G. and Chang, E. (1990) Proc Natl Acad Sci USA 87, 3324-7.
    5. Hirschfeld, S. et al. (1990) Mol Cell Biol 10, 2041-8.
    6. Payne, A. and Chu, G. (1994) Mutat Res 310, 89-102.
    7. Chu, G. and Chang, E. (1988) Science 242, 564-7.
    8. Nichols, A.F. et al. (1996) J Biol Chem 271, 24317-20.
    9. Kataoka, H. and Fujiwara, Y. (1991) Biochem Biophys Res Commun 175, 1139-43.
    10. Keeney, S. et al. (1992) Mutat Res 273, 49-56.
    11. He, Y.J. et al. (2006) Genes Dev 20, 2949-54.
    12. Lee, J. and Zhou, P. (2007) Mol Cell 26, 775-80.
    13. Wang, H. et al. (2006) Mol Cell 22, 383-94.
    14. Kapetanaki, M.G. et al. (2006) Proc Natl Acad Sci USA 103, 2588-93.
    15. Guerrero-Santoro, J. et al. (2008) Cancer Res 68, 5014-22.
    16. Ghosh, P. et al. (2008) Cell Cycle 7, 373-81.
    17. Hu, J. et al. (2008) Genes Dev 22, 866-71.
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