Render Target: STATIC
Render Timestamp: 2024-12-20T10:53:36.315Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-10-30 15:02:11.058
Product last modified at: 2024-12-17T18:47:43.398Z
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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.

SARM1 (D2M5I) Rabbit mAb #13022

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 73
    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

    SARM1 (D2M5I) Rabbit mAb recognizes endogenous levels of total human SARM1 protein and transfected levels of total mouse SARM1 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro324 of human SARM1 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.

    Sterile alpha and TIR motif-containing protein 1 (SARM1) is a TIR domain-containing adaptor protein that contains two sterile alpha motif (SAM) domains (15). SARM1 is the only known TIR domain-containing adaptor that does not activate NF-κB, but instead negatively regulates toll-like receptor signaling (16). Research studies suggest that SARM1 inhibits signaling by TLR3 and TLR4 through direct interaction with the TIR domain-containing adapter TRIF, which is required for TLR3 and MyD88-independent TLR4 signaling (16-18). Additional research indicates that SARM1 can mediate injury-induced axon death, neuronal cell death in response to infection with the encephalitis-causing La Crosse virus, and T cell death following an immune response to infection (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. Mink, M. et al. (2001) Genomics 74, 234-44.
    16. Carty, M. et al. (2006) Nat Immunol 7, 1074-81.
    17. Yamamoto, M. et al. (2002) J Immunol 169, 6668-72.
    18. Yamamoto, M. et al. (2003) Science 301, 640-3.
    19. Osterloh, J.M. et al. (2012) Science 337, 481-4.
    20. Mukherjee, P. et al. (2013) Immunity 38, 705-16.
    21. Panneerselvam, P. et al. (2013) Cell Death Differ 20, 478-89.
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