Amyloid β precursor protein (APP) is a type I transmembrane glycoprotein. The APP gene is mapped to human chromosome 21q21.3 and encodes various isoforms due to alternative splicing events. APP displays the ubiquitous expression, although, high levels are observed in the brain. It comprises a large ectodomain, short cytoplasmic tail, E1, and E2 domains. The E1 domain harbors a growth factor-like domain (GFLD) and a copper-binding domain (CuBD).
Peptide sequence around aa. 666-670 ( A-V-T-P-E ), according to the protein APP.
Anti-APP (Ab-668) antibody produced in rabbit has been used in:
- western blotting
Amyloid β precursor protein (APP) serves as a precursor of amyloid β (Aβ) peptide. It participates in synaptic function, trans-cellular synaptic adhesion, and in the anterograde transport of the virus.
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APP encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.
Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol
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