| Applications | WB, B/N |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | Alexa Fluor 647 |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human Dectin-1/CLEC7A (R&D Systems, Catalog # 1859-DC) Thr66-Met201 Accession # NP_072092 |
| Specificity | Detects human Dectin-1/CLEC7A in direct ELISAs and Western blots. In this format, less than 2% cross‑reactivity with recombinant mouse Dectin-1 and recombinant human Dectin-2 is observed. |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Purity Statement | Antigen Affinity-purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
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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