Human Dectin‑2/CLEC6A Antibody

Dectin-2, also known as CLEC6A, CLECSF10, and NKCL, belongs to the C-type lectin family of transmembrane immune regulatory glycoproteins. Dectin-2, plus CLEC4A-E constitute a subgroup of molecules that exhibit approximately 40% amino acid (aa) sequence identity in their extracellular domains (ECD), and have a conserved cysteine spacing in their carbohydrate recognition domains (CRD) (1, 2). Mature human Dectin-2 is a type II transmembrane protein with a short cytoplasmic tail, a transmembrane segment, and a 168 aa ECD with a stalk region and one CRD (3, 4). Within the ECD, human Dectin-2 shares 71% and 75% aa sequence identity with bovine and mouse Dectin-2, respectively. An alternately spliced beta isoform has a deletion of portions of the transmembrane and cytoplasmic regions (5). Full length Dectin-2 is a 27 kDa molecule that is expressed on monocytes, tissue macrophages, and activated CD4⁺ T cells (4‑6). The CRD of Dectin-2 contains an EPN motif which is characteristic of calcium-dependent mannose-binding lectins. Dectin-2 selectively interacts with high mannose structures in the Man₉GlcNAc₂ configuration (7). It mediates the recognition of a variety of microorganisms, particularly the filamentous forms of yeast and fungii (7, 8). The short cytoplasmic tail does not contain signaling motifs but mediates association with the ITAM-containing Fc receptor gamma subunit on macrophages (8). Ligation of Dectin-2 induces tyrosine phosphorylation of the gamma subunit, activation of NF kappa B, and enhanced release of TNF-alpha and IL-1ra (8). Macrophage Dectin-2 is up‑regulated in vivo by inflammatory stimuli and UV-B irradiation (5, 6, 9). Dectin-2 is known to participate in UV-induced immunosuppression by interacting with CD4⁺CD25⁺ regulatory T cells, which then induce dendritic cells to release IL-4, IL-10, and TGF-beta (10).