Fc gamma RIIIA/CD16a Protein, Human (CHO, His)

Fc gamma RIIIA/CD16a Protein serves as a receptor for the invariable Fc fragment of immunoglobulin gamma (IgG), optimally activated upon binding clustered antigen-IgG complexes displayed on cell surfaces, initiating antibody-dependent cellular cytotoxicity (ADCC). This process involves the lysis of antibody-coated cells, preventing inappropriate effector cell activation in the absence of an antigenic trigger. The protein mediates IgG effector functions on natural killer (NK) cells, binding antigen-IgG complexes generated during infection to trigger NK cell-dependent cytokine production and degranulation. Fc gamma RIIIA/CD16a is crucial in generating memory-like adaptive NK cells that efficiently eliminate virus-infected cells via ADCC. It regulates NK cell survival, proliferation, and prevents NK cell progenitor apoptosis. As an Fc-binding subunit, it associates with CD247 and/or FCER1G adapters to form functional signaling complexes, leading to intracellular signaling cascades that drive NK cell activation. The protein also plays a role in mediating the antitumor activities of therapeutic antibodies, triggering TNFA-dependent ADCC of IgG-coated tumor cells and enhancing ADCC in response to afucosylated IgGs. In the context of Dengue virus infection, Fc gamma RIIIA/CD16a is involved in pathogenesis through an antibody-dependent enhancement (ADE) mechanism, facilitating virus entry into myeloid cells and subsequent viral replication during secondary infections.