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Amyloid Precursor Protein (APP) or Amyloid beta precursor protein acts as a cell-surface membrane receptor called kinesin I responsible for the axonal transfer of beta-secretase and presenilin 1. APP is essential for neuronal growth, neurite adhesion, as well as the process of axonogenesis.
It is a 100-140kDa transmembrane glycoprotein which exists in multiple isoforms as a result of alternative splicing. The proteolytic cleavage of APP through secretases results in the production of beta amyloid which is the main part of plaques of senility. You can know more about beta Amyloid/APP antibody online.
The abnormal regulation and processing of the APP is also a factor with Down's syndrome early-onset familial Alzheimer's disease, as well as cerebral hemorrhage. Amyloid B (Ab) precursor protein (APP) is a transmembrane glycoprotein with a kDa range of 100 that can be found in several forms.
Its amino acid sequence of APP has the amyloid domain. It is released through the proteolytic cleavage process in two steps. The deposition of extracellular material and the accumulation of released Ab fragments are the primary elements of amyloid plaques in Alzheimer's disease. The APP protein can be phosphorylated in multiple sites, which can alter the proteolytic process and the release of the Protein.
The phosphorylation at Thr668 through cyclin-dependent kinase depends on the cell cycle and occurs in the G2/M phase. App phosphorylated at Thr668 occurs in the adult brains of rats and is associated with neuronal differentiation in culture.