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Render Timestamp: 2024-11-21T13:20:34.414Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-10-30 15:02:10.183
Product last modified at: 2024-11-13T18:00:09.028Z
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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.

Toll-like Receptor 7 (E4J3Z) Rabbit mAb #82658

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 74, 120, 140
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    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

    Toll-like Receptor 7 (E4J3Z) Rabbit mAb recognizes endogenous levels of total TLR7 protein, including the full-length protein that migrates at 140 kDa, the full-length deglycosylated protein that migrates at 120 kDa, and the C-terminal cleaved protein that migrates at 74 kDa.

    Species Reactivity:

    Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a recombinant protein fragment specific to mouse TLR7 protein.

    Background

    Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adapter proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adapter-like/TIR-associated protein (MAL/TIRAP), TIR domain-containing adapter-inducing IFN-β (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

    TLR7, 8 and 9 form a group of structurally related TLR family members that are localized to intracellular endosomes (15-17). TLR7 shows highest expression in lung, placenta, and spleen (15). TLR7 mediates responses to a class of synthetic compounds, including imidazoquinolines, guanosine-based drugs that induce anti-viral responses (18). TLR7 responds to ssRNA viruses to activate NF-κB and trigger IFN production (19-21).
    1. Akira, S. (2003) J Biol Chem 278, 38105-8.
    2. Beutler, B. (2004) Nature 430, 257-63.
    3. Dunne, A. and O'Neill, L.A. (2003) Sci STKE 2003, re3.
    4. Medzhitov, R. et al. (1997) Nature 388, 394-7.
    5. Schwandner, R. et al. (1999) J Biol Chem 274, 17406-9.
    6. Takeuchi, O. et al. (1999) Immunity 11, 443-51.
    7. Alexopoulou, L. et al. (2001) Nature 413, 732-8.
    8. Zhang, F.X. et al. (1999) J Biol Chem 274, 7611-4.
    9. Horng, T. et al. (2001) Nat Immunol 2, 835-41.
    10. Oshiumi, H. et al. (2003) Nat Immunol 4, 161-7.
    11. Muzio, M. et al. (1997) Science 278, 1612-5.
    12. Wesche, H. et al. (1997) Immunity 7, 837-47.
    13. Suzuki, N. et al. (2002) Nature 416, 750-6.
    14. Irie, T. et al. (2000) FEBS Lett 467, 160-4.
    15. Chuang, T.H. and Ulevitch, R.J. (2000) Eur Cytokine Netw 11, 372-8.
    16. Du, X. et al. (2000) Eur Cytokine Netw 11, 362-71.
    17. Heil, F. et al. (2003) Eur J Immunol 33, 2987-97.
    18. Hemmi, H. et al. (2002) Nat Immunol 3, 196-200.
    19. Heil, F. et al. (2004) Science 303, 1526-9.
    20. Diebold, S.S. et al. (2004) Science 303, 1529-31.
    21. Lund, J.M. et al. (2004) Proc Natl Acad Sci U S A 101, 5598-603.
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