Render Target: STATIC
Render Timestamp: 2024-11-22T11:23:04.092Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-11-18 16:03:18.149
Product last modified at: 2024-11-20T09:00:10.719Z
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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.

TRIF (F6K4E) Rabbit mAb #16809

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 98
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:200

    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

    TRIF (F4K4E) Rabbit mAb recognizes endogenous levels of total TRIF protein. This antibody detects a band of unknown origin at 37 kDa in some cell lines.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu220 of human TRIF 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.

    TRIF, also known as TIR domain-containing adapter molecule 1 (TICAM-1), is a TIR domain adapter protein described to activate NF-κB and IRF3 and trigger IFN-β production (15,16). Studies using dominant negative forms of TRIF and siRNA targeting TRIF show that TRIF functions downstream of TLR3 and TLR4 in response to dsRNA and LPS, respectively (15-17). TRIF recruits TRAF6-TAK1-TAB2 to the receptor complex, which leads to NF-κB activation (18). In addition, TRIF can trigger signaling that leads to the induction of apoptosis (19).
    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. Yamamoto, M. et al. (2002) J Immunol 169, 6668-72.
    16. Oshiumi, H. et al. (2003) Nat Immunol 4, 161-7.
    17. Fitzgerald, K.A. et al. (2003) J Exp Med 198, 1043-55.
    18. Jiang, Z. et al. (2004) Proc Natl Acad Sci USA 101, 3533-8.
    19. Kaiser, W.J. and Offermann, M.K. (2005) J Immunol 174, 4942-52.
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