>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Mouse TLR4 Fc Chimera is immobilized at 2 μg/mL, 100 μL/well, the concentration of
Human MD-2 (Catalog # 1787-MD)
that produces 50% of the optimal binding
response is approximately 0.15-0.9 μg/mL
When Recombinant Mouse TLR4 Fc Chimera (Catalog # 9149-TR) is coated at 2 µg/mL (100 μL/well), Recombinant Human MD-2 (Catalog # 1787-MD) binds with a typical ED50 of 0.15-0.9 μg/mL.
TLR4, also known as CD284, is a 100 kDa type I transmembrane glycoprotein that belongs to the mammalian Toll-Like Receptor family of pathogen pattern recognition molecules. The complex of TLR4 with MD-2 functions as a critical receptor for bacterial endotoxin/lipopolysaccharide (LPS) (1-3). Mature mouse TLR4 consists of a 613 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 176 aa cytoplasmic domain. TLR4 contains 19 leucine rich repeats in its ECD and one cytoplasmic Toll/IL-1 receptor (TIR) domain (4-6). Within the ECD, mouse TLR4 shares 63% and 83% aa sequence identity with human and rat TLR4, respectively. On monocytes, macrophages, dendritic cells, and B cells, MD‑2 expression is required for cell surface localization of TLR4 and for optimal LPS‑induced TLR4 signaling (7-10). MD‑2 also forms soluble disulfide-linked homo-oligomers which can interact with TLR4 (8). Through a domain separate from its TLR4-binding domain, MD‑2 extracts LPS from circulating CD14‑LPS complexes and carries the LPS into a ternary complex with TLR4 (11-13). The interaction of MD‑2/LPS with TLR4 induces receptor oligomerization and the triggering of an inflammatory response (2, 14). Increased levels of plasma MD‑2 in septic shock patients sensitizes MD‑2 non-expressing epithelial cells to LPS and promotes widespread tissue inflammation (15).
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