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Description
The monoclonal antibody 2A11 recognizes mouse β-glucan receptor, also known as dectin-1. Dectin- 1 is a small type II transmembrane receptor containing one lectin-like carbohydrate recognition domain. This domain recognizes β1,3- and/or β1,6-linked glucans, intact yeast and an immunoreceptor tyrosine-based activation motif (ITAM) in the cytoplasmic tail. β-Glucan is one of the most abundant polysaccharides in fungal pathogens. By recognizing β-glucan, dectin-1 has a fundamental function in antifungal immunity. Dectin-1 is a signaling non-Toll-like pattern-recognition receptor required for the induction of protective immune responses. Dectin-1 is responsible for the β- glucan-dependent, nonopsonic recognition of zymosan by primary macrophages. Zymosan is a yeast derived particle composed principally of polysaccharides, of which β-glucan and mannan are the major constituents. In vivo administration of zymosan, or purified soluble β-glucans, has a number of desirable effects on immune function, including the ability to confer resistance to tumors and various infections. The receptor is highly expressed on macrophages and neutrophils and to a lesser extent on dendritic cells and a subpopulation of T cells. Dectin-1 participates with the complement receptor CR3 in a host proinflammatory cytokine response to a fungal pathogen. The monoclonal antibody 2A11 recognizes an extracellular epitope on dectin-1.
Immunogen
NIH 3T3 cells transduced with full-length Dectin-1