||Recombinant human TLR-3 produced in293 cellsis 77.0 kDa glycoprotein containing 681 residues which comprise the TLR-3 extracellular domain.
||TLR-3 is a single-pass type I receptor that binds to and signals the presence of microbial pathogens and double stranded RNA (dsRNA) viruses. Signaling through TLR-3 can promote the NF-κB pathway to initiate innate and adaptive immune responses to bacterial and viral infections, as well as the p53 pathway to trigger apoptosis in cells infected with dsRNA viruses. TLR-3 belongs to a family of structurally-related toll-like receptors (TLRs) containing an N-terminal domain rich in leucine repeats and a C-terminal intracellular Toll/interleukin (IL)-1 (TIL) domain. TLR-3 is expressed primarily in dendritic cells of the placenta and pancreas where it can reside on both sides of the plasma membrane and in the endosomal compartment of the cells.
||95 % (SDS-PAGE, HPLC).
||< 0.1 ng per μg of TLR-3.
||Determined by its ability to inhibit IL-8 secretion induced by Poly I:C in the TLR3 receptor-expressing HEK293 cells (HEK293 TLR3r). The ED50for this effect is ≤ 30 μg/ml in the presence of 100 μg/ml of Poly I:C.
||The lyophilized protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted TLR-3 is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. Avoid repeated freeze-thaw cycles.