Amyloid precursor protein (APP) is encoded by the gene mapped to human chromosome 21. It is a transmembrane glycoprotein widely distributed in many tissues. APP exists as multiple isoforms (100-140 kDa) including APP695, APP751 and APP770 that are derived from alternative mRNA splicing.
synthetic peptide corresponding to an N-terminal region of human Amyloid Precursor Protein (APP), conjugated to KLH. The corresponding sequence is highly conserved (single amino acid substitution) in rat and mouse APP.
Anti-APP (N-terminal region) antibody produced in rabbit has been used in:
The amyloid precursor protein (APP) undergoes extensive post-translational modifications including phosphorylation, glycosylation, tyrosine sulfation and nitration. APP has been reported to be phosphorylated at several sites that may affect its processing and secretion. Phosphorylation of APP at Thr688 by cyclin-dependent kinase 5 (Cdk5) has been shown to play a critical role in the proteolytic cleavage of APP. APP Thr688, phosphorylated form is found in the adult brain and it correlates with neuronal differentiation. Mutations in the APP gene are linked with rare forms of autosomal dominant familial Alzheimer′s disease (FAD). These mutations result in increased production of Aβ indicating a central role of Aβ peptide in the neuropathology of AD.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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