Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind biotinylated Laminarin (1, 3-beta -glucan) in a functional ELISA with an estimated KD <6 nM. |
Source | Mouse myeloma cell line, NS0-derived mouse Dectin-1/CLEC7A protein Phe69-Leu244, with an N-terminal 10-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | Clec7a |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 21.6 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 27-37 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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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