This product is an unconjugated, non-therapeutic recombinant analog of the anti-FcRn antibody batoclimab, produced for research use only and built around the human neonatal Fc receptor (FcRn) target. It is not the clinical drug and is not intended for human or veterinary use. Batoclimab is a fully human IgG1 antibody that binds the neonatal Fc receptor and blocks the site where FcRn engages the Fc region of IgG, thereby shortening the half-life of circulating IgG, including pathogenic autoantibodies. As a research reagent, this analog is useful as a positive control and benchmarking tool in FcRn-binding and IgG-recycling assays, for comparability and bridging studies against in-house anti-FcRn candidates, for epitope-competition and blocking experiments, and for cell-based and biochemical characterization of FcRn interactions. It is supplied at research grade with low endotoxin (typically under 1 EU/mg, with an ultra-low option under 0.5 EU/mg) and is available in bulk milligram-to-gram quantities to support assay development, in-vitro mechanistic work, and preclinical characterization. No clonal identity is implied.
The neonatal Fc receptor (FcRn), encoded by FCGRT (UniProt P55899) and paired with beta-2-microglobulin, is an MHC class I-like receptor that governs the long serum half-life of IgG and albumin. After fluid-phase endocytosis, IgG binds FcRn in a strictly pH-dependent manner: engagement of the IgG Fc CH2-CH3 interface is strong in the acidic endosome (around pH 6) and negligible at near-neutral blood pH. Bound IgG is diverted away from lysosomal degradation and recycled back to the cell surface, where the neutral extracellular pH triggers release. This salvage pathway, together with a parallel albumin-binding site, extends IgG persistence and mediates transcytosis across epithelia, including maternal-to-fetal transfer. Blocking FcRn removes this protection, accelerating catabolism of total IgG and, therapeutically, of pathogenic autoantibodies.