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Render Timestamp: 2024-11-21T13:38:45.738Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-10-30 15:02:10.784
Product last modified at: 2024-11-11T23:30:09.538Z
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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 9 (D2C9) Rabbit mAb #5845

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 130
    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 1:100

    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 9 (D2C9) Rabbit mAb recognizes endogenous levels of total TLR9 protein. This antibody is predicted to react with known full-length isoforms of TLR9, but not with the cleaved TLR9 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the central ectodomain of human TLR9 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.

    TLR9 is highly expressed in macrophages, dendritic cells, and B lymphocytes, and in humans has five isoforms generated by alternative splicing (15,16). TLR9 binds to unmethylated CpG motifs present on bacterial DNA and stimulates NF-κB via the MyD88 adaptor protein (17-19). In contrast to most TLR family members that are localized to the plasma membrane, TLR9 is an intracellular receptor localized to the ER in resting cells (20). Upon binding to CpG DNA, TLR9 is proteolytically processed and translocates to endo-lysosomal compartments where it binds MyD88, initiating downstream signaling (21-23).
    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. Du, X. et al. (2000) Eur Cytokine Netw 11, 362-71.
    16. Chuang, T.H. and Ulevitch, R.J. (2000) Eur Cytokine Netw 11, 372-8.
    17. Hemmi, H. et al. (2000) Nature 408, 740-5.
    18. Bauer, S. et al. (2001) Proc Natl Acad Sci U S A 98, 9237-42.
    19. Takeshita, F. et al. (2001) J Immunol 167, 3555-8.
    20. Latz, E. et al. (2004) Nat Immunol 5, 190-8.
    21. Park, B. et al. (2008) Nat Immunol 9, 1407-14.
    22. Ewald, S.E. et al. (2008) Nature 456, 658-62.
    23. Sepulveda, F.E. et al. (2009) Immunity 31, 737-48.
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