Recombinant Human Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A), partial (Active)

CD16a (FCGR3A) mediates antibody-dependent cellular cytotoxicity by engaging the Fc region of IgG1, making it a critical target for therapeutic antibody optimization and Fc-engineering campaigns. This recombinant human FCGR3A extracellular domain (aa 17–208) carries the V176 polymorphism—the high-affinity variant—and demonstrates confirmed binding to human IgG1 Fc with a KD of 0.571 μM by BLI, providing a suitable basis for affinity characterization, competitive inhibition assays, and blocking antibody screening. Mammalian cell expression preserves native glycosylation patterns essential for proper folding and physiologically relevant receptor-ligand interactions, supporting use in therapeutic antibody epitope mapping, Fc-variant ranking by SPR or BLI, and biologic inhibitor screening. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based ADCC reporter assays and sensitive binding studies where contaminant interference must be minimized.