Mouse Dectin-1/CLEC7A APC-conjugated Antibody Summary
Phe69-Leu244
Accession # Q6QLQ4
Applications
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.
Scientific Data
Detection of Dectin‑1/CLEC7A in Mouse Blood Monocytes by Flow Cytometry. Mouse whole blood monocytes were stained with Rat Anti-Mouse Gr-1/Ly-6G PE-conjugated Monoclonal Antibody (Catalog # FAB1037P) and either (A) Rat Anti-Mouse Dectin-1/CLEC7A APC-conjugated Monoclonal Antibody (Catalog # FAB17561A) or (B) Rat IgG2AAllophycocyanin Isotype Control (Catalog # IC006A). View our protocol for Staining Membrane-associated Proteins.
Detection of Dectin‑1/CLEC7A in Raw264.7 Mouse Cell Line by Flow Cytometry. Mouse Raw264.7 monocyte/macrophage cell line was stained with Rat Anti-Mouse Dectin-1/CLEC7A APC-conjugated Monoclonal Antibody (Catalog # FAB17561A, filled histogram) or Rat IgG2A Isotype Control (IC006A, open histogram). Staining was performed using our Staining Membrane-associated Proteins protocol.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: Dectin-1/CLEC7A
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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