epitope corresponding to amino acids 161-250 mapping within an N-terminal extracellular domain of TLR1 of human origin
Modification Notes
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. TLR1, as well as the other TLR family members, is a type I transmembrane receptor that characteristically contains 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. Expression of TLR receptors is highest in peripheral blood leukocytes, macrophages and monocytes. TLR6 is highly homologous to TLR1, sharing greater than 65% sequence identity, and, like other members of TLR family, it induces NF˚B signaling upon activation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of TLR1 of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 161-250 mapping within an N-terminal extracellular domain of TLR1 of human origin
Tissue Specificity
epitope corresponding to amino acids 161-250 mapping within an N-terminal extracellular domain of TLR1 of human origin