Pan-amyloid-beta (1-40) is one of several functional peptides (39 to 43 amino acids in length) formed from proteolytic cleavage of the amyloid-beta precursor protein (APP) by the family of secretase enzymes. Although the APP protein is required for a number of biological functions, including axonal transport, cell adhesion, and transcription, the Ab 1-40 peptide has been studied mostly for its potential to aggregate and form neurite plaques, which may contribute to neurotoxicity, particularly in the context of neurodegenerative disease such as Alzheimer's. Previous studies have demonstrated that Anti-pan amyloid beta peptide (MOAB2), clone 6C3 detects specifically amyloid-beta, but not APP. Furthermore MOAB2 detects multiple amyloid-beta 40 and amyloid-beta 42 conformations including unaggregated, oligomeric and fibrillar. In a number of immunohistochemical and biochemical analyses, MOAB2 consistently detected intraneuronal amyloid-beta, but not APP, and showed greater specificity to amyloid-beta than 6E10. MOAB2 is therefore suitable for sensitive and specific detection of accumulating amyloid-beta peptides in Alzheimer's disease models.