Analysis Biomolecular Interactions of His-tagged Mouse FcγRIIb and FcγRIII with Anti-penta-His by BLI (CAT#: STEM-MB-0122-CJ)

Introduction

Soluble immune complexes containing IgG1 Fc can suppress ongoing autoimmunity in a variety of animal models. For example, OVA-anti-OVA conjugates, aggregated intravenous immunoglobulin (IVIG) products, and antibody-coated liposomes are therapeutically efficacious in murine models of idiopathic thrombocytopenic purpura (ITP) and rheumatoid arthritis. The translational relevance of these animal findings is supported by clinical studies in ITP, in which the therapeutic effects of IVIG directly correlate with the presence of immune aggregates in the sera.

The Fc portion of immunoglobulin G (IgG) is a horseshoe-shaped homodimer, which interacts with various effector proteins, including Fcγ receptors (FcγRs). These interactions are critically dependent on the pair of N-glycans packed between the two CH2 domains. The main function of FcγRIIB is to inhibit activating signals. This leads to phosphorylation of the cytoplasmic domain ITIM of FcγRIIB by the Src-family kinase lYN29.