The Toll-like receptor (TLR) family in mammal comprises a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain ａnd IL-1 receptor motif in the cylasmic domain. Like its counterparts in Drosophila, TLRs signal through adaptor molecules. The TLR family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition. Ten human homologs of TLRs (TLR1-10) have been described. Among this family of receptors, TLR2 ａnd TLR4 have been most studied. These studies have suggested that TLR2 ａnd TLR4 may serve as potential main mediators of LPS signaling (4,5). The TLR4 cDNA codes for a protein consisting of 799 amino acids with approximate molecular weight of 88 kDa. Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection ａnd serve as an important link between the innate ａnd adaptive immune responses. These proteins act through adaptor molecules such as MyD88 ａnd TIRAP to activate various kinases ａnd transcription factors such as Protein Kinase C (PKC) alpha/beta ａnd NF-κB. Studies with TLR4-deficient mice indicate that the main ligand for TLR is lipopolysaccharide. Consequently, these mice also showed increased susceptibility to Gram-negative sepsis.
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TLR4 monoclonal antibody was raised against a portion of amino acids 100 - 200 of TLR4 (Human).

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