Anti-mAB-O | Mouse anti-human Abeta protein (3-10) region, oligomer-specific (clone 3E5,F8)

Dot blot reaction of the binding capacity of mAB-O to fibrils, monomers and oligomers. Equal amounts of each sample were spotted on a nitrocellulose membrane and then dried. The membrane was blocked with 5% non-fat milk before incubated for 1 h with anti-mAB-O (25nM) and then with secondary antibody, anti-mouse HRP-conjugated (1:1500). The membrane was washed with PBS containing 0.25% Tween-20 before detection using ECL prime (GE Healthcare).

Immunolocalization: human tissue was paraffin-embedded and sectioned. De-waxed and rehydrated in an ethanol gradient. Antigens were retrieved in sodium citrate buffer (pH 6) at 95°C for 1 h. The tissue sections were separately incubated for 1 h at RT with primary antibody and antibody binding was visualized with IgG Preoxidase Reagent Kit.

This Monoclonal IgG1, kappa light chain, (clone number 3E5.F8) is specific for human Amyloid-Beta oligomers.

Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein. Recent findings however suggest that smaller oligomeric forms of Abeta, formed in parallel to the amyloid plaques, excert the predominant tissue damaging effect.

Specific identification of the oligomeric forms is as a consequence of great interest. Based on a recently published technique a highly oligomer-specific antibody (mAB-O), targeting Abeta oligomers while omitting reactivity towards the monomeric and fibrillar counterpart, has been developed.