Recombinant Human Dectin-1/CLEC7A Fc Chimera Protein, CF Summary
Accession # Q9BXN2.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human Dectin-1/CLEC7A Fc Chimera (Catalog # 10364-DC) is immobilized at 0.25 μg/mL (100 μL/well), Biotinylated Laminarin (1, 3-beta-glucan) binds with an ED50 of 0.08-9.6 ng/mL.
2 μg/lane of Recombinant Human Dectin-1/CLEC7A Fc Chimera (Catalog # 10364-DC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 54-64 kDa and 108-128 kDa, respectively.
Dectin-1, also known as CLEC7A and the beta -glucan receptor, is a 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 (ECD) (3, 4). Alternate splicing generates one major isoform expressed on the surface of monocytes, macrophages, myeloid DC, neutrophils, eosinophils, B cells, and CD4+ T cells that lacks the stalk region (3-6). The mature ECD of human Dectin-1 shares 59% and 57% amino acid (aa) sequence identity with mouse and rat Dectin-1, respectively. The CRD of Dectin-1 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).
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Citation for Recombinant Human Dectin-1/CLEC7A Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Alteration of microbiota antibody-mediated immune selection contributes to dysbiosis in inflammatory bowel diseases
Authors: E Michaud, L Waeckel, R Gayet, R Goguyer-De, B Chanut, F Jospin, K Bathany, M Monnoye, C Genet, A Prier, C Tokarski, P Gérard, X Roblin, N Rochereau, S Paul
Embo Molecular Medicine, 2022;0(0):e15386.
Sample Types: Recombinant Protein
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