epitope corresponding to amino acids 27-326 mapping within an N-terminal extracellular domain of TLR5 of mouse 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) (1,2). 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 (3). 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 (4). TLR2 and TLR4 are activated in response to lipopolysacchride (LPS) stimulation, which results in the activation and translocation of NFkB and suggests that these receptors are involved in mediating inflammatory responses (5,6). TLR5 specifically participates in the innate immune response to microbial agents. TLR5 is highly expressed in ovary and in peripheral blood leukocytes, most abundantly in monocytes and, to a lesser extent, in prostate and testis.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of TLR5 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 27-326 mapping within an N-terminal extracellular domain of TLR5 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 27-326 mapping within an N-terminal extracellular domain of TLR5 of mouse origin