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Render Timestamp: 2024-10-09T09:42:06.024Z
Commit: f04ddd7fea9fb3592f59f61482fcb94610d25cbe
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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 3 (D10F10) Rabbit mAb #6961

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 115-130
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    Toll-like Receptor 3 (D10F10) Rabbit mAb recognizes endogenous levels of total TLR3 protein. A band is detected at 75 kDa in some cell lines/tissues which is of unknown origin.

    Species Reactivity:

    Human

    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:

    Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val495 of human TLR3 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 adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (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.
    TLR3 functions as a receptor for double-stranded (ds)RNA typically associated with viral infection (4). It was originally shown to be specifically expressed in dendritic cells of the leukocyte family (5). TLR3 has also been found in placenta and lung, and can be induced by LPS in a variety of tissues (4,6). TLR3 is predominantly localized to early endosomes (7,8). Binding of dsRNA, or the analog polyinosine-polycytidylic acid (pIpC), to TLR3 triggers activation of transcription factors NF-κB and IRF3 through the adaptor protein TICAM-1/TRIF (9,10). TRIF associates with members of the TRAF family and with RIP that combine to activate NF-κB and IRF3 (11-13).
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    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. Alexopoulou, L. et al. (2001) Nature 413, 732-8.
    16. Muzio, M. et al. (2000) J Immunol 164, 5998-6004.
    17. Nishimura, M. and Naito, S. (2005) Biol Pharm Bull 28, 886-92.
    18. Matsumoto, M. et al. (2003) J Immunol 171, 3154-62.
    19. Funami, K. et al. (2007) J Immunol 179, 6867-72.
    20. Hoebe, K. et al. (2003) Nat Immunol 4, 1223-9.
    21. Oshiumi, H. et al. (2003) Nat Immunol 4, 161-7.
    22. Sasai, M. et al. (2010) Mol Immunol 47, 1283-91.
    23. Meylan, E. et al. (2004) Nat Immunol 5, 503-7.
    24. Jiang, Z. et al. (2004) Proc Natl Acad Sci USA 101, 3533-8.
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