Dectin-1/CLEC7A Protein, Human (HEK293)

Dectin-1/CLEC7A Protein operates as a lectin, functioning as a pattern recognition receptor (PRR) specifically designed for beta-1,3-linked and beta-1,6-linked glucans, prominent constituents of cell walls in pathogenic bacteria and fungi. Essential for the Toll-like receptor 2 (TLR2)-mediated inflammatory response, Dectin-1, upon binding to beta-glucan, recruits spleen tyrosine kinase (SYK) via its immunoreceptor tyrosine-based activation motif (ITAM) and instigates a signaling cascade. This cascade activates CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 pathways. Consequently, the stimulation of gene expression encoding pro-inflammatory cytokines and chemokines ensues, thereby enhancing cytokine production in macrophages and dendritic cells. Beyond its role in inflammation, Dectin-1 mediates the production of reactive oxygen species and is instrumental in the phagocytosis of Candida albicans conidia. Moreover, Dectin-1 binds T-cells, playing a role in T-cell activation, inducing phosphorylation of SCIMP upon beta-glucan binding. Existing as a homodimer, Dectin-1 interacts with SYK, participating in leukocyte activation in the presence of fungal pathogens.