The binding sites on human IgG1 for human Fcγ receptor (FcγR) I, FcγRIIa, FcγRIIb, FcγRIIIa
and neonatal FcR have been mapped. A common set of IgG1 residues is involved in binding …

Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated
immune responses with cellular effector functions. A high resolution map of the binding site …

We are investigating the interactions of recombinant human IgG antibodies with Fc receptors
to enable selection of a constant region giving minimal depletion of antigen-bearing cells …

Abstract The Fc variant of IgG2, designated as IgG2σ, was engineered with
V234A/G237A/P238S/H268A/V309L/A330S/P331S substitutions to eliminate affinity for Fcγ …

Recombinant monoclonal antibodies have entered the clinic as effective in vivo therapeutic.
A majority of the therapeutics antibodies employed are intact IgG molecules. IgG …

Antibody fragments are emerging as promising biopharmaceuticals because of their
relatively small size and other unique properties. However, compared with full-size …

Interactions between human IgG with human FcγRI and FcγRIIa (R131) were studied to
investigate the role of the hinge region of IgG3 and IgG1 in the binding of the antibodies to …

Recombinant human IgG antibodies (hIgGs) completely devoid of binding to Fcγ receptors
(FcγRs) and complement protein C1q, and thus with abolished immune effector functions …

To characterize the region on human IgG1 responsible for its high-affinity interaction with the
human Fc gamma receptor class I (Fc gamma RI), we have analyzed the binding properties …

Human IgG is the main antibody class used in antibody therapies because of its efficacy and
longer half-life, which are completely or partly due to FcγR-mediated functions of the …