Mouse Dectin-1/CLEC7A Alexa Fluor® 594-conjugated Antibody Summary
Accession # Q6QLQ4
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Dectin‑1/CLEC7A in HEK293 Human Cell Line transfected with Mouse Dectin-1/CLEC7A by Flow Cytometry. HEK293 cell line transfected with Mouse Dectin-1/CLEC7A (filled histogram) or irrelevant protein (open histogram) was stained with Rat Anti-Mouse Dectin‑1/CLEC7A Alexa Fluor® 594‑conjugated Monoclonal Antibody (Catalog # FAB17561T). Staining was performed using our Staining Membrane-associated Proteins protocol.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Dectin-1, also known as CLEC7A and the beta -glucan receptor, is a 43 kDa type II transmembrane C-type lectin that functions in the innate immune response to fungal pathogens. Although Dectin-1 resembles other CLEC molecules structurally, it binds ligands in a calcium-independent manner (1, 2). Mature mouse Dectin-1 is a 244 amino acid (aa) glycoprotein that consists of a short ITAM-containing cytoplasmic tail, a transmembrane segment, and a stalk and carbohydrate recognition domain (CRD) in the extracellular domain (3). The CRD of mouse Dectin-1 shares 61%, 60%, and 87% aa sequence identity with that of bovine, human, and rat Dectin‑1, respectively. It shares 25%‑34% aa sequence identity with the CRD of other subgroup members CLEC-1, CLEC-2, CLEC9A, CLEC12B, LOX-1, and MICL. Mouse Dectin-1 is alternately spliced, generating a variant that lacks the stalk region (4). Mouse Dectin-1 is expressed on monocytes, macrophages, and neutrophils, and on some populations of dendritic cells and T cells (5). It is upregulated on macrophages by GM-CSF, IL-4, or IL-13 and downregulated by dexamethasone, IL-10, or LPS (6). The CRD selectively binds beta -glucan polymers, a major component of yeast and mycobacterial cell walls (7). Yeast beta -glucan is accessible to Dectin-1 only at sites of cell budding, and Dectin-1 does not recognize the filamentous form of yeast (8). Dectin-1 mediates the phagocytosis of zymosan particles and intact yeast (8‑10). It co-localizes with TLR2 in the presence of zymosan, and the two receptors cooperate in ligand recognition and the propagation of proinflammatory signaling (9, 11‑13). Dectin-1 interaction with the tetraspanin CD37 increases its stability on the cell membrane and inhibits ligand-induced signaling (14). Genetic knockout of Dectin-1 in mice increases their susceptibility to pathogenic infection (15, 16).
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