MD2 Protein, Cynomolgus (His)

MD2 protein binds bacterial lipopolysaccharide (LPS) and collaborates with TLR4 in the innate immune response to LPS. It also interacts with TLR2 in the response to cell wall components from bacteria. MD2 enhances TLR4-dependent NF-kappa-B activation and forms a heterogeneous homomer, participating in a multi-protein complex with CD14 and TLR4. Ligand binding induces complex oligomerization, crucial for the cellular response to LPS. MD2 Protein, Cynomolgus (His) is the recombinant cynomolgus-derived MD2 protein, expressed by E. coli , with C-His labeled tag. The total length of MD2 Protein, Cynomolgus (His) is 142 a.a., with molecular weight of 17.97 kDa.

MD2 Protein, a key player in the innate immune response, serves as a critical component in recognizing bacterial lipopolysaccharide (LPS) and coordinating immune reactions. It binds directly to LPS and collaborates with TLR4 to elicit the innate immune response to bacterial LPS. Moreover, MD2 works in tandem with TLR2, responding to cell wall components from both Gram-positive and Gram-negative bacteria. MD2's interaction with TLR4 enhances NF-kappa-B activation, emphasizing its role in signaling pathways. In cell contexts expressing both LY96 and TLR4, MD2 enables responsiveness to LPS, underlining its importance in the cellular recognition of bacterial components. Structurally, MD2 forms a heterogeneous homomer from homodimers linked by disulfide bonds and is a crucial component of the lipopolysaccharide (LPS) receptor complex, which includes at least CD14, LY96, and TLR4. MD2's ligand binding induces interactions with TLR4 and promotes the oligomerization of the complex, further highlighting its central role in the immune response to bacterial challenges.

Cynomolgus

E. coli

C-His

B3Y6B0 (Q19-N160)

102118398

17.97 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.