This product is an unconjugated, non-therapeutic recombinant analog of the anti-FcRn antibody nipocalimab, supplied strictly for research use only. It is a fully recombinant human IgG1-lambda protein built around the same molecular target, the neonatal Fc receptor (FcRn, encoded by FCGRT, UniProt P55899), and is intended as a laboratory reagent rather than as the clinical drug. It is not for human or veterinary use. The analog is useful for researchers studying FcRn biology, IgG homeostasis, and antibody half-life engineering: it serves as a defined positive control in FcRn-binding and IgG-recycling assays, as a benchmarking or reference molecule in comparability and bioanalytical method development, and as a tool for probing the FcRn-IgG interaction in vitro. Because it is offered at research grade with low endotoxin levels and in bulk milligram-to-gram quantities, it supports higher-throughput screening, structure-function studies, and preclinical model work where consistent, well-characterized material is needed. Ultra-low-endotoxin options support endotoxin-sensitive cell-based and functional assays.
FcRn (neonatal Fc receptor) is a non-classical MHC class I-like molecule composed of an FCGRT-encoded alpha chain (UniProt P55899) non-covalently associated with beta-2-microglobulin. It binds the Fc region of IgG and also albumin in a strictly pH-dependent manner: binding is tight in the acidic environment of the endosome (around pH 6) and released at near-neutral extracellular pH (around 7.4). Through this pH switch, FcRn rescues pinocytosed IgG and albumin from lysosomal degradation and recycles them back to the cell surface, extending their serum half-life. FcRn also mediates transcytosis of IgG across epithelial and placental barriers, contributing to maternal-to-fetal antibody transfer and mucosal immunity. Blocking the IgG-binding site on FcRn accelerates catabolism of circulating IgG, including pathogenic autoantibodies, which is the rationale behind FcRn-antagonist drug development.