This product is an unconjugated, non-therapeutic recombinant analog of aducanumab, supplied for research use only. It is a fully human IgG1 monoclonal antibody directed against aggregated forms of beta amyloid, the peptide derived from amyloid precursor protein (APP, UniProt P05067) that accumulates in Alzheimer's disease. It reproduces the target specificity of the originator molecule while being manufactured independently of any clinical program; it is not the licensed drug and is not intended for human or veterinary use. The format makes it a useful tool for in-vitro and preclinical work: as a well-characterized positive control or reference binder in aggregation and immunodetection assays, for studying antibody recognition of amyloid conformers, and as a benchmark in comparability, ADCC/effector, or engineering studies. It is offered at research grade with low endotoxin (<1 EU/mg; ultra-low <0.5 EU/mg options) and in bulk milligram-to-gram quantities, supporting assay development, screening, and preclinical model work where consistent lot-to-lot supply and defined specificity matter.
Beta amyloid (Abeta) is a short peptide, chiefly 40 or 42 residues long, released from the transmembrane amyloid precursor protein (APP, UniProt P05067) by sequential cleavage by beta-secretase (BACE1) and the gamma-secretase complex. Monomeric Abeta can self-associate into soluble oligomers, protofibrils, and insoluble fibrils that deposit as the extracellular plaques characteristic of Alzheimer's disease. The longer, more hydrophobic Abeta42 species is especially aggregation-prone. Soluble oligomeric and fibrillar assemblies are widely implicated in synaptic dysfunction, neuroinflammation, and neuronal injury, making conformation-specific recognition biologically important. Antibodies such as aducanumab preferentially bind aggregated Abeta (oligomers and fibrils) over monomer, a selectivity relevant to distinguishing pathological assemblies from physiological peptide and to studying the amyloid cascade in vitro and in animal models.