Detects human Dectin‑1/CLEC7A in direct ELISAs. In directs ELISAs, less than 10% cross-reactivity with recombinant human (rh) DLEC and no cross-reactivity with recombinant mouse Dectin-1 or rhDectin-2 is observed.
Monoclonal Mouse IgG2B Clone # 259931
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human Dectin‑1/CLEC7A Thr66-Met201 Accession # NP_072092
Supplied in a saline solution containing BSA and Sodium Azide.
PerCP (Peridinin-chlorophyll Protein Complex)
10 µL/106 cells
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 Human Blood Monocytes by Flow Cytometry. Human peripheral blood monocytes were stained with Mouse Anti-Human Dectin‑1/CLEC7A PerCP‑conjugated Monoclonal Antibody (Catalog # FAB1859C, filled histogram) or isotype control antibody (Catalog # IC0041C, open histogram). 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 33 kDa type II transmembrane C-type lectin that participates in the innate immune response to fungal pathogens. Although Dectin-1 structurally resembles other CLEC molecules, it binds its ligands in a calcium-independent manner (1, 2). Mature human Dectin-1 consists of a short N-terminal ITAM-containing cytoplasmic tail, a transmembrane segment, and a C-terminal stalk with a carbohydrate recognition domain (CRD) in the extracellular domain (3, 4). Alternate splicing generates one major splice form that lacks the stalk region (3‑5). This isoform is expressed on the surface of monocytes, macrophages, myeloid DC, neutrophils, eosinophils, B cells, and CD4+ T cells (6). The CRD selectively binds beta -glucan polymers, a major component of yeast and mycobacterial cell walls (5‑7). Yeast beta -glucan is accessible to Dectin‑1 only during the process of cell budding. Dectin-1 does not recognize the filamentous form of yeast (8). Dectin-1 mediates the phagocytosis of zymosan particles and intact yeast (8‑10). In the membrane, Dectin-1 colocalizes 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 also interacts with tetraspanin CD37. This increases its stability on the cell membrane and inhibits ligand-induced signaling (14). Dectin-1 knockout mice show increased susceptibility to pathogenic infection (15‑16). The CRD of human Dectin-1 shares 77%, 60%, and 60% amino acid (aa) sequence identity with that of bovine, mouse and rat Dectin-1, respectively. It shares 29%‑39% aa sequence identity with the CRD of other subgroup members, including CLEC-1, CLEC-2, CLEC9A, CLEC12B, LOX-1, and MICL.
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