Product Pathways - NF-kappaB Signaling
MyD88 Antibody #3699
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IF-IC | H Mk | Endogenous | 33 | Rabbit |
Applications Key:
W=Western Blotting
IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:
H=Human
Mk=Monkey
Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
MyD88 Antibody detects endogenous levels of total MyD88 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding lysine 119 of human MyD88. Antibodies were purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from HeLa cells, either mock transfected or transfected with MyD88, using MyD88 Antibody.
Western Blotting
Western blot analysis of extracts from Jurkat, K562 and Raji cells, using MyD88 Antibody.
IF-IC
Immunofluorescent staining of HeLa cells transfected with MyD88 showing punctate localization, using MyD88 Antibody.
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 (1-3). TLRs recognize conserved motifs found in various pathogens and mediate defense responses. Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes. The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the TIR domain. Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains including MyD88 (myeloid differentiation factor), MAL/TIRAP (MyD88-adaptor-like/TIR-associated protein), TRIF (Toll-receptor-associated activator of interferon) and TRAM (Toll-receptor-associated molecule). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK. Activation of IKK leads to the degradation of IκB that normally maintains NF-κB inactivity by sequestering it in the cytoplasm.
MyD88 was originally isolated as a myeloid differentiation primary response gene that is rapidly induced upon IL-6 stimulated differentiation of M1 myeloleukemic cells into macrophages (4-6). It contains an amino-terminal death domain separated from a carboxyl-terminal TIR domain and functions as an adaptor in TLR/IL-1 receptor signaling (7). The death domain of MyD88 mediates interactions with the IRAK complex triggering a signaling cascade that includes the activation of NF-κB (8,9).
- Akira, S. (2003) J Biol Chem 278, 38105-8.
- Beutler, B. (2004) Nature 430, 257-63.
- Dunne, A. and O'Neill, L.A. (2003) Sci STKE 2003, re3.
- Harroch, S. et al. (1995) Nucleic Acids Res. 23, 3539-46.
- Hardiman, G. et al. (1996) Oncogene 13, 2467-75.
- Bonnert, T.P. et al. (1997) FEBS Lett. 402, 81-4.
- Medzhitov, R. et al. (1998) Mol. Cell 2, 253-8.
- Wesche, H. et al. (1997) Immunity 7, 837-47.
- Muzio, M. et al. (1997) Science 278, 1612-1615.
Application References
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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.
