Detects mouse Dectin‑1/CLEC7A in direct ELISAs and Western blots. In Western blots, approximately 10% cross-reactivity with recombinant human (rh) Dectin-1 is observed and no cross-reactivity with recombinant mouse Dectin-2 or rhDLEC is observed.
Monoclonal Rat IgG2A Clone # 218820
Protein A or G purified from hybridoma culture supernatant
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 Alexa Fluor® 700‑conjugated Monoclonal Antibody (Catalog # FAB17561N) or (B) Rat IgG2A Alexa Fluor 700 Isotype Control (Catalog # IC006N). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
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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