Amyloid Beta 1-42 Oligomer Antibody, Clone 2F9: Biotin

Amyloid beta (Aβ) peptide, particularly the 1-42 isoform (Aβ1-42), plays a central role in the pathogenesis of Alzheimer’s disease (AD) . Aβ is generated through proteolytic cleavage of the amyloid precursor protein (APP) and can self-assemble into a range of aggregated species, including oligomers, protofibrils, fibrils, and ultimately extracellular plaques. Among these, Aβ1-42 oligomers are increasingly recognized as the most neurotoxic species, contributing to synaptic dysfunction, neuroinflammation, and cognitive decline. Our amyloid beta oligomer antibody has been validated for high specificity toward Aβ1-42 oligomers, distinguishing them from other aggregated forms. This specificity is critical for accurately detecting early-stage, soluble aggregates that precede plaque formation and are believed to drive early neurodegenerative changes in AD (1) . The immunogen used to generate these oligomers was Amyloid Beta Peptide 1-42, pre-treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP), following established protocols to ensure reproducible oligomer formation (2, 3) . This preparation method enhances the structural fidelity of oligomeric species, enabling more precise investigation of their pathological roles. Given that most therapeutic strategies over the past two decades have targeted Aβ accumulation, tools that selectively recognize Aβ1-42 oligomers are essential for advancing both basic research and translational efforts in Alzheimer’s disease.

Amyloid Beta 1-42 Oligomer, Aβ1-42 Oligomer, Abeta Oligomers, Amyloid beta peptide 1-42, Aβ42, Beta-amyloid protein 42, Beta-APP42, Amyloid beta A4 protein, APP, ABPP, APPI, Non-A4 component of amyloid precursor, Alzheimer disease amyloid protein

A 1:10,000 dilution of SMC-620 was sufficient for detection of 1ug of AB 1-42 oligomers by western blot analysis with goat-anti-rabbit:HRP as the secondary and ELISA analysis (capture at 1 ug/mL, 6E10:HRP used as the detection at 0.25ug/mL) .

1. Panza et al. 2019. Nat Rev Neurol. 15:73-88 https://doi.org/10.1038/s41582-018-0116-6 2. Stine et al. 2003. JBC. 278(13):11612-22. doi: 10.1074/jbc.M210207200 3. Ahmed et al. 2010. Nature Structural & Molecular Biology. 17(5):561 doi: 10.1038/nsmb.1799

1. Panza et al. 2019. Nat Rev Neurol. 15:73-88 https://doi.org/10.1038/s41582-018-0116-6 2. Stine et al. 2003. JBC. 278 (13) :11612-22. doi: 10.1074/jbc.M210207200 3. Ahmed et al. 2010. Nature Structural & Molecular Biology. 17 (5) :561 doi: 10.1038/nsmb.1799