Dectin-1/CLEC7A Protein, Mouse (HEK293, Fc)

The Dectin-1/CLEC7A protein operates as a lectin, specifically recognizing beta-1,3-linked and beta-1,6-linked glucans found in the cell walls of pathogenic bacteria and fungi. Essential for the Toll-like receptor 2 (TLR2)-mediated inflammatory response, Dectin-1/CLEC7A activates NF-kappa-B by recruiting spleen tyrosine kinase (SYK) through its immunoreceptor tyrosine-based activation motif (ITAM). This initiates a signaling cascade involving the CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 pathways. Consequently, this cascade stimulates the expression of genes encoding pro-inflammatory cytokines and chemokines. Additionally, Dectin-1/CLEC7A enhances cytokine production in macrophages and dendritic cells, mediates the production of reactive oxygen species, and facilitates the phagocytosis of C. albicans conidia. Notably, it binds to T-cells independently of their surface glycans, playing a role in T-cell activation, stimulating T-cell proliferation, and inducing SCIMP phosphorylation upon beta-glucan binding. The protein forms homodimers and interacts with SYK, contributing to leukocyte activation in the presence of fungal pathogens.