TLR1 Fc Chimera, Recombinant, Human (Toll-like receptor 1, CD281, DKFZp547I0610, DKFZp564I0682, KIAA0012, MGC104956, MGC126311, MGC126312, rsc786, TIL, Toll/interleukin-1 receptor-like protein)

Catalog No : USB-T8050-04B
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Product name TLR1 Fc Chimera, Recombinant, Human (Toll-like receptor 1, CD281, DKFZp547I0610, DKFZp564I0682, KIAA0012, MGC104956, MGC126311, MGC126312, rsc786, TIL, Toll/interleukin-1 receptor-like protein)
Catalog No USB-T8050-04B
Supplier’s Catalog No T8050-04B
Supplier US Biologicals
Source antigen NSO cells
Reactivity
Cross reactivity
Applications
Molecular weight
Storage -20°C
Other names
Grade Highly Purified
Purity ≥ 90% by SDS-­PAGE under reducing conditions and visualized by silver stain. Endotoxin: ≤1.0 EU/ug protein (LAL method).
Form Lyophilized from a 0.2um filtered solution in PBS. Reconstitute with 500ul sterile PBS.
Reactivity life 6 months
Note For reserch purpose only
Purity ≥ 90% by SDS-­PAGE under reducing conditions and visualized by silver stain. Endotoxin: ≤1.0 EU/ug protein (LAL method).
Description 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 Fκ 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).