This is clone 3G8, a mouse IgG1 kappa monoclonal antibody raised against human CD16 (FcgammaRIII), one of the most widely used and best-characterized anti-CD16 clones. It recognizes human CD16 and is validated for IHC on frozen sections, flow cytometry, immunoprecipitation, functional blocking, and CyTOF (mass cytometry), making it a versatile reagent for immunophenotyping and functional studies of NK cells, monocyte/macrophage subsets, and granulocytes. As a human-reactive antibody, it is suited to in-vitro and ex-vivo functional research rather than mouse in-vivo depletion or blockade models. Supplied in bulk (mg to gram scale) as a research-grade, low-endotoxin (<1 EU/mg) preparation, it supports demanding applications where high antibody mass, lot consistency, and low endotoxin matter, such as receptor-blocking assays, ADCC/CD16-crosslinking experiments, primary human cell isolation, and metal-conjugated CyTOF panels. For research use only (RUO). The 3G8 clone is a common benchmark, easing comparison with the published literature.
CD16 is a low-affinity Fc receptor for IgG (FcgammaRIII) that binds the Fc region of IgG immune complexes and antibody-opsonized targets. It exists as two closely related genes: FcgammaRIIIa (CD16a, UniProt P08637), a transmembrane signaling receptor expressed on NK cells, monocytes, macrophages, and some T-cell subsets, and FcgammaRIIIb (CD16b), a GPI-anchored form on neutrophils. On NK cells, CD16a is the principal trigger of antibody-dependent cellular cytotoxicity (ADCC): Fc engagement drives signaling through associated CD3zeta and FcRgamma ITAM chains, promoting cytotoxic granule release and cytokine production. CD16a is subject to activation-induced shedding by ADAM17, which modulates NK effector function. A well-known FcgammaRIIIa polymorphism (V158F) alters IgG binding affinity and correlates with clinical responses to therapeutic antibodies, making CD16 central to studies of ADCC and antibody effector function.