Six human homologs of the Drosophila Toll receptor were initially identified based on their sequence similarities and designated Toll-like receptors (TLR). Toll receptors are involved in mediating dorsoventral polarization in the developing Drosophila embryo and also participate in the host immunity. The TLR family of proteins are characterized by a highly conserved Toll homology (TH) domain, which is essential for Toll-induced signal transduction. Expression of TLR receptors is highest in peripheral blood leukocytes, macrophages and monocytes. TLR1, as well as the other TLR family members, are type I transmembrane receptors that characteristically contain an extracellular domain consisting of several leucine-rich regions along with a single cytoplasmic Toll/IL-1R-like domain. TLR2 and TLR4 are activated in response to lipopolysacchride (LPS) stimulation, which results in the activation and translocation of NF˚B and suggests that these receptors are involved in mediating inflammatory responses. TLR3 is highly expressed in placenta and pancreas, and is limited to the dendritic subpopulation of leukocytes. TLR3 recognizes dsRNA associated with viral infection and induces activation of NF˚B and production of type I interferons, which suggests that it may play a role in host defense against viruses. TLR6 is highly homologous to TLR1, sharing greater than 65% sequence identity. Like other members of TLR family, TLR6 induces NF˚B signaling upon activation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
ELISAIFIPWB
WB:1:100~1:500 IP:1:20~1:100 IF:1:20~1:100
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 26-325 mapping within an N-terminal extracellular domain of TLR3 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 26-325 mapping within an N-terminal extracellular domain of TLR3 of mouse origin