>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
50 kDa (Pro form) & 47 kDa (Mature form). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Beta-site amyloid precursor protein cleaving enzyme 1
Beta-site APP cleaving enzyme 1
beta-site APP-cleaving enzyme 1
beta-site APP-cleaving enzyme
Membrane-associated aspartic protease 2
transmembrane aspartic proteinase Asp2
BACE-1 is an aspartic protease and an integral membrane protein (1-5). BACE-1 is the peptidase predominantly responsible for cleavage of the amyloid precursor protein beta site in the brain to generate the amyloid beta peptide. Because the amyloid beta peptide is a major component of amyloid plaques, BACE-1 has been implicated in the onset and/or progression of Alzheimer's disease. BACE-1 is expressed in a variety of human tissues. It is likely that this peptidase has functions in addition to its hydrolysis of the amyloid precursor protein. The peptidase activity of BACE-1 is optimal under mildly acidic conditions (pH 3.5-5.5), consistent with its proposed function in an acidic intracellular compartment.
Ermolieff, J. et al. (2000) Biochemistry 39:12450.
Lin, X. et al. (2000) Proc. Natl. Acad. Sci. USA 97:1456.
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