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Render Timestamp: 2024-10-25T10:35:54.285Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-08-01 15:32:11.726
Product last modified at: 2024-10-15T11:45:14.804Z
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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.

Exportin-1/CRM1 (D6V7N) Rabbit mAb #46249

Filter:
  • WB
  • IP
  • IHC
  • IF

    Supporting Data

    REACTIVITY H M Mk
    SENSITIVITY Endogenous
    MW (kDa) 123
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunohistochemistry (Paraffin) 1:300 - 1:1200
    Immunofluorescence (Immunocytochemistry) 1:400 - 1:1600

    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.

    For a carrier free (BSA and azide free) version of this product see product #49000.

    Protocol

    Specificity / Sensitivity

    Exportin-1/CRM1 (D6V7N) Rabbit mAb recognizes endogenous levels of total exportin-1/CRM1 protein.

    Species Reactivity:

    Human, Mouse, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human exportin-1/CRM1 protein.

    Background

    Exportins are a family of seven proteins that are responsible for intracellular transport. Exportin-1, also known as chromosome region maintenance 1 (CRM1), is a protein essential for nuclear export of hundreds of proteins, mRNAs, and rRNAs (1-3). Exportin-1 binds to substrates with nuclear export signals (NESs) rich in leucine and other hydrophobic amino acids (4). These hydrophobic sequences form an alpha-helix-loop that can bind to the exportin-1 hydrophobic groove (5). Studies have shown that these NESs can be modified either by protein modifications or by mutation to regulate exportin-1 binding (6-7). Targets of exportin-1 include many tumor suppressors, such as Rb, p53, FoxO1, BAF47, as well as oncoproteins, such as p21 and p27 (1). In addition, Myc can upregulate exportin-1 during biogenesis, where it can export newly formed 40S and 60S subunits from the nucleoli (8-9).

    Inhibition of nuclear export has been pursued for therapeutic application since the finding that leptomycin B could suppress HIV replication by suppressing the ability of exportin-1 to export the HIV-1 protein Rev (2, 10). Overexpression of exportin-1 has been associated with poor prognosis in various cancer types (11-13). Genomic approaches and development of inhibitors have identified exportin-1 as a druggable target (14-16). The use of various inhibitors of exportin-1 is also being explored in various antiviral therapies (17-18).
    1. Xu, D. et al. (2012) Mol Biol Cell 23, 3673-6.
    2. Ossareh-Nazari, B. et al. (1997) Science 278, 141-4.
    3. Fukuda, M. et al. (1997) Nature 390, 308-11.
    4. Kutay, U. and Güttinger, S. (2005) Trends Cell Biol 15, 121-4.
    5. Dong, X. et al. (2009) Nat Struct Mol Biol 16, 558-60.
    6. Vogt, P.K. et al. (2005) Cell Cycle 4, 908-13.
    7. Craig, E. et al. (2002) EMBO J 21, 31-42.
    8. Thomas, F. and Kutay, U. (2003) J Cell Sci 116, 2409-19.
    9. Golomb, L. et al. (2012) Mol Cell 45, 222-32.
    10. Wolff, B. et al. (1997) Chem Biol 4, 139-47.
    11. Noske, A. et al. (2008) Cancer 112, 1733-43.
    12. Shen, A. et al. (2009) Neurosurgery 65, 153-9; discussion 159-60.
    13. Yao, Y. et al. (2009) Oncol Rep 21, 229-35.
    14. Schmidt, J. et al. (2013) Leukemia 27, 2357-65.
    15. Boyle, S.M. et al. (1999) J Virol 73, 6872-81.
    16. Walker, C.J. et al. (2013) Blood 122, 3034-44.
    17. Yadav, V. et al. (2016) Virusdisease 27, 357-368.
    18. Chutiwitoonchai, N. et al. (2017) Virology 507, 32-39.
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