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DR647MS) and counterstained with DAPI (blue; Lunaphore Catalog # DR100). Specific staining was localized to the membrane and cyoplasm. Protocol available in COMET™ Panel Builder." class="big_lightbox" target="_blank">
DR647MS) and counterstained with DAPI (blue; Lunaphore Catalog # DR100). Specific staining was localized to the membrane and cyoplasm. Protocol available in COMET™ Panel Builder." class="big_lightbox" target="_blank">
DR647MS) and counterstained with DAPI (blue; Lunaphore Catalog # DR100). Specific staining was localized to the membrane and cyoplasm. Protocol available in COMET™ Panel Builder." class="big_lightbox" target="_blank">
MAB0041, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG F(ab')2Secondary Antibody (Catalog # F0102B)." class="big_lightbox" target="_blank">
FAB141F). Quadrant markers were set based on control antibody staining (Catalog # MAB0041)." class="big_lightbox" target="_blank">
10504-DC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 44-54 kDa." class="big_lightbox" target="_blank">
DC-SIGN encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. The encoded protein is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity. Variations in the number of 23 amino acid repeats in the neck domain of this protein are rare but have a significant impact on ligand binding ability. This gene is closely related in terms of both sequence and function to a neighboring gene (GeneID 10332; often referred to as L-SIGN). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.