Special remarks: Human Amyloid-beta N-terminal specific.
  Reacts with both soluble and fibrillar Abeta to a similar degree
  No cross reaction with non-cleaved APP
  No cross reaction with mouse and rat.

Alzheimer’s disease (AD) was first reported by A. Alzheimer, a German neuropathologist in 1906 and is considered as a major factor of dementia. Senile plaque observed in the Alzheimer brain consists of Amyloid beta (A-beta). It is reported that the A-beta protein consists of 40-42 (43) amino acids. And that it is cleaved from Amyloid Precursor Protein (APP, which exists in three main isoforms, APP695, APP751, and APP770) by beta-secretase and subsequent gamma-sevretase.
Reports have shown that many variants of A-beta exist and are clarified into the culture supernatant from the APP cDNA transfected mouse neuroblastoma cell. And further, in 1995, Saido et al have found A-beta (N3pE) which is a molecular species distinct from the standard A-beta, and which is deposited in the brain in a dominant and differential manner. A-beta (N3pE) starts at the 3^rd aminoterminal residue of the standard A-beta, glutamate, converted to pyroglutamate through intramolecular dehydration.