mAB-M | Mouse anti-human Abeta protein (3-10) region, oligomer-specific (clone 2D10,F6)

synthetic peptide chosen from human Abeta protein (3-10) pregion, oligomer specific

IHC used to illustrate the lack of binding of mAB-M to plaques. Tissue sections from the human AD hippocampus were de-waxed and rehydrated in ethanol and then incubated with AS08 357 (A) and mAB-M(B) at RT for 1h. The immunoreactivity was detected with the anti-mouse Peroxidase Reagent Kit (ImmPRESS, Vector Laboratories, Inc.) and then developed using the ImmPACT AEC Peroxidase Substrate kit (Vector Laboratories, Inc.).

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.

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-M), targeting Abeta oligomers while omitting reactivity towards the monomeric and fibrillar counterpart, has been developed.