CD14 Protein, Human (Biotinylated, HEK293, His-Avi)

CD14 serves as a crucial coreceptor for bacterial lipopolysaccharide (LPS), playing a pivotal role in the innate immune response to microbial pathogens. In collaboration with LBP, CD14 binds monomeric LPS and facilitates its delivery to the LY96/TLR4 complex, initiating downstream signaling events. This process involves the activation of MyD88, TIRAP, and TRAF6, leading to NF-kappa-B activation, cytokine secretion, and the inflammatory response. Additionally, CD14 acts as a coreceptor for TLR2:TLR6 and TLR2:TLR1 heterodimers in response to diacylated and triacylated lipopeptides, respectively, with these clusters triggering signaling and subsequently translocating to the Golgi in a lipid-raft dependent pathway. CD14's interaction with electronegative LDL (LDL(-)) contributes to the cytokine release induced by LDL(-). CD14 is an integral component of the lipopolysaccharide (LPS) receptor complex, collaborating with LY96 and TLR4. Furthermore, it interacts with various partners, such as LPS-bound LBP, LPAR1, MYO18A, and FSTL1, underscoring its multifaceted role in immune responses and lipid metabolism.