Amyloid-B Monoclonal Antibody (Clone 6C3, MOAB-2)

Amyloid plaques composed primarily of the 42 amino acid form of amyloid-? peptide (A?42) are a hallmark of Alzheimer’s disease (AD). However, the roles of the various amyloid ? peptide(s), especially A?42, related to the neurotoxicity characteristic of AD remains unclear. A major hindrance to evaluating the role of A? in AD pathology has been the availability of anti-A? antibodies to selectively detect A? versus amyloid precursor protein (APP), A?40 versus A?42, and specific conformations of the peptide, particularly oligomeric forms. MOAB-2 (mouse IgG2b) is a pan-specific antibody specific to A? (residues 1-4) that differentiates intracellular A? from APP. MOAB-2 does not detect APP in cell culture media/lysates or in brain homogenates from transgenic mice expressing 5 familial AD mutation (5xFAD mice). Intraneuronal A? was confirmed by co-localization of MOAB-2 immunoreactivity with C-terminal antibodies specific for A?40 and A?42, and with cathepsin-D, a lysosomal marker. Additionally, MOAB-2 demonstrates strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.{20683}