TLR7 Protein, Human (His, Myc)

TLR7 Protein serves as an endosomal receptor with a pivotal role in both innate and adaptive immunity. Its function involves orchestrating the host immune response against pathogens by recognizing uridine-containing single-strand RNAs (ssRNAs) of viral origin or guanosine analogs. Upon binding to agonists, TLR7 undergoes dimerization, facilitating the direct contact of Toll/Interleukin-1 receptor (TIR) domains and leading to the recruitment of the downstream adapter MYD88 through homotypic interaction. This initiates the formation of the Myddosome signaling complex involving IRAK4, IRAK1, TRAF6, and TRAF3, culminating in the activation of downstream transcription factors NF-kappa-B and IRF7. This cascade induces the production of pro-inflammatory cytokines and interferons, crucial for mounting an effective immune response. TLR7 exhibits activation not only by uridine-containing single-strand RNAs but also by guanosine analogs, such as deoxyguanosine, 7-thia-8-oxoguanosine, or 7-deazaguanosine, in a RNA-independent manner. Additionally, imiquimod is recognized as an activator of TLR7, further emphasizing its diverse and integral role in immune signaling pathways.