TLR7 Protein, Mouse (His, Myc)

The TLR7 protein is an endosomal receptor critical in innate and adaptive immunity that recognizes uridine-containing single-stranded RNA (ssRNA) or guanosine analogs in viruses, thereby controlling the host immune response. Upon agonist binding, TLR7 dimerizes, activates the Myddosome complex and recruits downstream adapters. TLR7 Protein, Mouse (His) is the recombinant mouse-derived TLR7 protein, expressed by E. coli , with C-His labeled tag.

The TLR7 protein is an endosomal receptor that plays a crucial role in both innate and adaptive immunity. It controls 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, bringing TIR domains from the two molecules into direct contact and leading to the recruitment of the downstream adapter MYD88 through homotypic interaction. This results in the formation of the Myddosome signaling complex, involving IRAK4, IRAK1, TRAF6, and TRAF3, ultimately leading to the activation of downstream transcription factors NF-kappa-B and IRF7. Activation of these transcription factors induces the production of pro-inflammatory cytokines and interferons, respectively. TLR7 can be activated by guanosine analogs, such as deoxyguanosine, 7-thia-8-oxoguanosine, or 7-deazaguanosine, in a RNA-independent manner.

Mouse

E. coli

N-10*His;C-Myc

P58681 (F27-S348)

170743  [NCBI]

Partial

FRWFPKTLPCEVKVNIPEAHVIVDCTDKHLTEIPEGIPTNTTNLTLTINHIPSISPDSFRRLNHLEEIDLRCNCVPVLLGSKANVCTKRLQIRPGSFSGLSDLKALYLDGNQLLEIPQDLPSSLHLLSLEANNIFSITKENLTELVNIETLYLGQNCYYRNPCNVSYSIEKDAFLVMRNLKVLSLKDNNVTAVPTTLPPNLLELYLYNNIIKKIQENDFNNLNELQVLDLSGNCPRCYNVPYPCTPCENNSPLQIHDNAFNSLTELKVLRLHSNSLQHVPPTWFKNMRNLQELDLSQNYLAREIEEAKFLHFLPNLVELDFS

≥ 85%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.