TLR3 Protein, Mouse (HEK293, His)

TLR3 protein is an important component of innate and adaptive immunity and can recognize pathogen-associated molecular patterns and activate NF-κ-B, IRF3 and cytokine secretion. Ligand binding induces TLR3 dimerization, and efficient signal transduction requires clustering of signaling units along the ligand. TLR3 Protein, Mouse (HEK293, His) is the recombinant mouse-derived TLR3 protein, expressed by HEK293 , with C-His labeled tag.

TLR3 protein serves as a key component in both innate and adaptive immunity, playing a pivotal role in the host immune response against pathogens by recognizing specific molecular patterns associated with microorganisms. Activated by double-stranded RNA, a characteristic feature of viral infection, TLR3 functions through the adapter TRIF/TICAM1, leading to NF-kappa-B activation, nuclear translocation of IRF3, cytokine secretion, and initiation of the inflammatory response. TLR3 exists as a monomer and homodimer, with ligand-binding triggering dimerization. The signaling unit comprises one approximately 40 bp ds-RNA and two TLR3 molecules, requiring lateral clustering of signaling units along the ds-RNA ligand for effective signal transduction. Interaction with UNC93B1, SRC, and TICAM1, particularly in response to poly(I:C), contributes to its regulatory functions, highlighting the intricate molecular mechanisms involved in TLR3-mediated immune responses.

Mouse

HEK293

C-His

Q99MB1/NP_569054.2 (T26-L705)

142980  [NCBI]

Lumenal Domain

TNQCTVRYNVADCSHLKLTHIPDDLPSNITVLNLTHNQLRRLPPTNFTRYSQLAILDAGFNSISKLEPELCQILPLLKVLNLQHNELSQISDQTFVFCTNLTELDLMSNSIHKIKSNPFKNQKNLIKLDLSHNGLSSTKLGTGVQLENLQELLLAKNKILALRSEELEFLGNSSLRKLDLSSNPLKEFSPGCFQTIGKLFALLLNNAQLNPHLTEKLCWELSNTSIQNLSLANNQLLATSESTFSGLKWTNLTQLDLSYNNLHDVGNGSFSYLPSLRYLSLEYNNIQRLSPRSFYGLSNLRYLSLKRAFTKQSVSLASHPNIDDFSFQWLKYLEYLNMDDNNIPSTKSNTFTGLVSLKYLSLSKTFTSLQTLTNETFVSLAHSPLLTLNLTKNHISKIANGTFSWLGQLRILDLGLNEIEQKLSGQEWRGLRNIFEIYLSYNKYLQLSTSSFALVPSLQRLMLRRVALKNVDISPSPFRPLRNLTILDLSNNNIANINEDLLEGLENLEILDFQHNNLARLWKRANPGGPVNFLKGLSHLHILNLESNGLDEIPVGVFKNLFELKSINLGLNNLNKLEPFIFDDQTSLRSLNLQKNLITSVEKDVFGPPFQNLNSLDMRFNPFDCTCESISWFVNWINQTHTNISELSTHYLCNTPHHYYGFPLKLFDTSSCKDSAPFEL

Approximately 85-110 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by Bis-Tris PAGE.

<1 EU/μg, determined by LAL method.