TLR1 Fc Chimera, Recombinant, Human (Toll-like receptor 1, CD281, DKFZp547I0610, DKFZp564I0682, KIAA

The Toll­like family of molecules are type I transmembrane proteins that serve as pattern recognition receptors for microbial pathogens. There are at least eleven mouse and ten human TLRs that activate the innate immune system following exposure to a variety of microbial species (1, 2) . TLRs contain a large number of leucine­rich repeats (LRRs) and a cytoplasmic tail with one Tol l /IL­1 receptor (TIR) domain. Mature human TLR1 consists of a 556 amino acid (aa) extracellular domain (ECD) with 20 LRRs, a 21 aa transmembrane segment, and a 185 aa cytoplasmic domain (3, 4). Within the ECD, human TLR1 shares 63% aa sequence identity with human TLR6 and 20% ­43% aa sequence identitity with human TLR2, ­3 , ­4 , ­5 , ­7 , ­8 , ­9, and ­10. It shares 73% and 71% aa sequence identity with mouse and rat TLR1, respectively. TLR1 is expressed on the surface of macrophages, dendritic cells, and tonsillar epithelial cells in ligand­independent association with TLR2 (5 ­ 8). TLR2 additionally associates with TLR6 to form a functional complex with specificity for distinct but related microbial ligands (9­11). TLR1 and TLR2 cooperate in the recognition of bacterial and protozoal triacylated lipopeptides and glycosyl phosphatidylinositols (6,10­12). Ligand binding induces TLR1 localization to lipid rafts followed by receptor internalization and activation of N Fkappa B (7,11,13). Description: NSO-expressed recombinant protein corresponding to human TLR1(Ser22 Asn578, Accession#AAC34137) linked using the sequence SIEGRMD to human IgG1 (Pro100 Lys330). Structure: Disulfide linked homodimer, N-terminal Sequence Analysis: Ser22, Molecular Mass: Predicted: 89.9kD, Observed: 95-105kD, (SDS-PAGE, reducing conditions), Activity: Measured by its ability to bind biotinylated Pam3CysSerLys4 (PAM3CSK4)., ,