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BACE1 (beta-secretase) is a key enzyme involved in the production of amyloid beta-peptides (Abeta) found in extracellular amyloid plaques of Alzheimer's disease (AD). In some cases early onset familial AD can be attributed to a "Swedish" mutation in the amyloid precursor protein (APP), which dramatically enhances the cleavage of this protein by BACE1. This and other genetic and pathological evidence has led to therapeutic approaches that have focused on the inhibition of BACE1 and other APP-cleaving enzymes, such as gamma-secretase stuff. APP is first cleaved by b-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for g-secretase to generate the 4 kDa amyloid-b peptide, which is deposited in the brains of all sufferers of Alzheimer's disease. The long-sought b-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). bACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
100 µg
100 µg
150 µL
100 µg
100 µL
100 µL
100 Tests
100 Tests
100 µL
100 µL
50 µg
100 µL
100 µL
100 µL
100 µL
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