This product is an unconjugated, non-therapeutic recombinant analog of rozanolixizumab, supplied strictly for research use only (not for human or veterinary use). Rozanolixizumab is a humanized IgG4 monoclonal antibody that binds the neonatal Fc receptor (FcRn) and blocks its interaction with the Fc region of IgG, thereby accelerating the degradation of circulating IgG including pathogenic autoantibodies. The research-grade analog reproduces the binding specificity of the originator against human FcRn, making it a useful tool for interrogating FcRn biology, antibody recycling, and IgG homeostasis in vitro and in preclinical systems. Typical applications include use as a reference or positive-control anti-FcRn binder in receptor-binding and blocking assays, as a benchmarking reagent in FcRn-dependent transcytosis and recycling studies, and as a comparator in biosimilarity or assay-development workflows. It is offered at research grade with low endotoxin (<1 EU/mg; ultra-low <0.5 EU/mg options), and is available in bulk milligram-to-gram quantities for scale-dependent experiments. It is an analog built around the FcRn target, not the clinical drug.
FcRn, the neonatal Fc receptor, is encoded by FCGRT (UniProt P55899) and functions as a heterodimer of an MHC class I-like alpha chain paired with beta-2-microglobulin. Unlike classical Fc-gamma receptors, FcRn binds the Fc region of IgG in a strictly pH-dependent manner: it engages IgG in acidified early endosomes (pH ~6.0) after fluid-phase uptake, then releases it at neutral extracellular pH (~7.4). This cycle rescues internalized IgG and albumin from lysosomal degradation and recycles them back to the circulation, giving IgG its characteristically long serum half-life and maintaining IgG and albumin homeostasis. FcRn also mediates transcytosis of IgG across epithelial and endothelial barriers, including maternal-fetal transfer. Blocking FcRn shortens IgG half-life and lowers total IgG, the rationale behind therapeutic FcRn antagonism in IgG-mediated autoimmune disease.