Mouse Dectin‑2/CLEC6A alpha Isoform Biotinylated Antibody

Dectin-2 alpha, also known as CLEC6A, CLECSF10, and NKCL, belongs to the C-type lectin family of transmembrane immune regulatory glycoproteins. Dectin-2 alpha, CLEC4A/DCIR, CLEC4B/DCAR, CLEC4C/DLEC, CLEC4D/MCL, and CLEC4E/mincle constitute a subgroup of these 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 mouse Dectin-2 alpha consists of a short cytoplasmic tail, a transmembrane segment, and an ECD with a stalk region and one CRD (3, 4). Alternate splicing leads to partial deletion of the transmembrane segment and stalk ( beta isoform) or a portion of the CRD ( gamma isoform) (4). The full length Dectin-2 alpha isoform is a 27 kDa molecule that is primarily expressed on the surface of tissue macrophages and their precursors (3‑6). The CRD of Dectin-2 alpha contains an EPN motif which is characteristic of calcium-dependent mannose-binding lectins. Dectin-2 alpha 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 in macrophages (8). Ligation of Dectin-2 alpha 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 alpha is upregulated in vivo by inflammatory stimuli and UV-B irradiation (6). It mediates the breaking of UV-induced tolerance by interacting with CD4⁺CD25⁺ regulatory T cells which then induce dendritic cells to release IL-4, IL-10, and TGF-beta (9). Within the ECD, mouse Dectin-2 alpha shares 71% aa sequence identity with human and bovine Dectin-2.