This product is an unconjugated, non-therapeutic recombinant analog of ponezumab, supplied strictly for research use only. Ponezumab is a humanized monoclonal antibody directed against the amyloid-beta (Abeta) peptide, a proteolytic fragment released from the amyloid-beta precursor protein (APP; UniProt P05067). It was investigated as a passive-immunotherapy candidate for Alzheimer disease, engineered to bind soluble Abeta and promote peripheral clearance. The research-grade analog reproduces the antigen-binding specificity of the originator so that laboratories can use it as a defined tool reagent rather than as a clinical drug. It is useful as a positive control and reference binder in Abeta ELISA, immunodepletion, and neutralization assays; as a benchmarking reagent in comparability, epitope-mapping, and antibody-engineering work; and as a standardized input for aggregation and clearance studies in cell-based and preclinical systems. It carries an engineered effector-attenuated Fc (Human IgG2 with A330S/P331S), matching the low-ADCC/CDC design of the originator. Material is offered at research grade with low endotoxin and in bulk milligram-to-gram quantities. It is not the clinical drug and is not for human or veterinary use.
The amyloid-beta precursor protein (APP; UniProt P05067) is a single-pass type I transmembrane glycoprotein broadly expressed in neurons and other tissues, where it contributes to cell adhesion, synapse formation, and signaling. Sequential proteolysis governs its fate: alpha-secretase within the amyloidogenic region yields soluble sAPP-alpha, whereas beta-secretase (BACE1) followed by gamma-secretase liberates the amyloid-beta (Abeta) peptides, principally Abeta40 and the more aggregation-prone Abeta42. These peptides self-associate into soluble oligomers and fibrils that deposit as extracellular plaques, a defining neuropathological feature of Alzheimer disease. Ponezumab does not target the full-length APP holoprotein but rather binds the free C-terminus of the Abeta40 peptide, a neo-epitope exposed after gamma-secretase cleavage. This specificity underlies its intended mechanism of engaging soluble Abeta to facilitate clearance while minimizing binding to intact membrane-anchored APP.