MyD88 Recombinant Rabbit Monoclonal Antibody [PSH09-74]

Function

Interleukin-1 (IL-1)-induced activation of the NFκB pathway is mediated through the IL-1 receptor and the subsequent phosphorylation of IL-1 receptor-associated kinase (IRAK). The myeloid differentiation protein MyD88 was originally characterized as a protein upregulated in myeloleukemic cells following IL-6-induced growth arrest and terminal differentiation. MyD88 is now known to function as an adaptor protein for the association of IRAK with the IL-1 receptor. MyD88 is functionally homologous to the adaptor protein tube in the Toll signaling pathway of Drosophilia, and both proteins are members of the Toll/IL-1R superfamily. MyD88 contains a characteristic N-terminal death domain that is essential for NFκB activation and an adjacent Toll/IL-1R homology domain (TIR domain). Collectively, these domains enable the protein-protein interactions of MyD88 with IRAK and the IL-1 receptor complex.

Background References

1. Kim, JE. et al. 2014. Paclitaxel-exposed ovarian cancer cells induce cancer-specific CD4+ T cells after doxorubicin exposure through regulation of MyD88 expression. International journal of oncology. 44: 1716-26.

2. Steinhagen, F. et al. 2013. IRF-5 and NF-κB p50 co-regulate IFN-β and IL-6 expression in TLR9-stimulated human plasmacytoid dendritic cells. Eur. J. Immunol. 43: 1896-1906.

Subcellular Location

Cytoplasm.

UNIPROT

SwissProt: Q99836 Human

SwissProt: P22366 Mouse

SwissProt: Q6Y1S1 Rat

Synonyms