CLEC4D Protein, Human (HEK293, His)

CLEC4D, a calcium-dependent lectin, operates as a pattern recognition receptor (PRR) in the innate immune system, discerning both damage-associated molecular patterns (DAMPs) and pathogen-associated molecular patterns (PAMPs) from bacteria and fungi. Recognizing alpha-mannans on C. albicans hyphae and mycobacterial trehalose 6,6'-dimycolate (TDM), CLEC4D forms a functional complex with the signaling adapter Fc receptor gamma chain/FCER1G, likely through its interaction with CLEC4E, in myeloid cells. Binding of TDM or C. albicans alpha-mannans to this receptor complex induces the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, activating SYK, CARD9, and NF-kappa-B. This activation drives the maturation of antigen-presenting cells and influences antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. CLEC4D, when forming a heterodimer with CLEC6A, exhibits activity against fungal infections. Additionally, it functions as an endocytic receptor, suggesting a role in antigen uptake at the site of infection, either for antigen clearance or for processing and subsequent presentation to T-cells. The heterodimerization with CLEC4E and CLEC6A further highlights the dynamic and versatile nature of CLEC4D in immune surveillance and response mechanisms.