beta Amyloid (C-Terminal) Rabbit anti-Human, Mouse, Polyclonal, Proteintech

Amyloid beta peptide (Abeta) is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimer′s disease. This peptide is generated from the beta-amyloid precursor protein (beta APP) in a two-step process. The first step involves cleavage of the extracellular, amino-terminal domain of beta APP. Protein cleavage is performed by an aspartyl protease termed beta-secretase (BACE). This enzyme is synthesized as a propeptide that must be modified to the mature and active form by the prohormone convertase, furin. Beta APP cleavage by the mature form of BACE results in the cellular secretion of a segment of beta APP and a membrane-bound remt. This remt is then processed by another protease termed gamma-secretase. Gamma-secretase cleaves an intra-membrane site in the carboxyl-terminal domain of beta APP, thus generating the amyloid beta peptide. Gamma-secretase is believed to be a multi-subunit complex containing presenilin-1 and 2 as central components. Found associated with the presenilins is the transmembrane glycoprotein nicastrin. Nicastrin has been found to bind to the carboxyl-terminus of betaAPP and helps to modulate the production of the amyloid beta peptide Also found in the neurofibrillary lesions in Alzheimer′s disease is the protein termed Tau. Tau is a neuronal microtubule-associated protein found predomitly on axons. The function of tau is to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), which is the building block of neurofibrillary lesions in Alzheimer′s disease brain.