The Amyloid-beta ELISA is a solid-phase sandwich ELISA that uses two highly specific antibodies to human amyloid-beta variants; one antibody is precoated onto the ELISA plate and the other is HRP-conjugated. Takara's Amyloid-beta ELISA can be used to measure human amyloid-beta protein variants in EDTA-plasma, cerebrospinal fluid, serum, cell culture media or brain extract.
The accumulation of amyloid-beta protein in the cerebral cortex is responsible for plaque formation and is thought to result in Alzheimer's disease (AD). Amyloid-beta is produced by the proteolytic cleavage of amyloid precursor protein (APP) and is mediated by the enzymes beta- and gamma-secretase. This cleavage reaction produces a number of peptides ranging from 36 to 43 amino acids in length. The Human Amyloid-beta ELISA can detect all amyloid-beta variants that are cleaved at the C-terminal side; however, it cannot detect variants fewer than 16 amino acids in length.