The membrane-associated aspartic protease BACE-1 (β-site APP cleaving enzyme, Asp2 or memapsin 2) has been identified as β-secretase. BACE-1 constitutes the predominant β-secretase activity in human brain tissue. It is highly expressed in neurons, the major site of Aβ generation. BACE-1 is localized within the Golgi and endosomal compartments, among the several intracellular sites where Aβ is thought to be produced. BACE-1 is initially an inactive proenzyme and localized in endoplasmic reticulum.
synthetic peptide corresponding to the N-terminus of human BACE-1 (amino acids 46-62).
Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit has been used in western blotting.
Overexpression of β-site APP cleaving enzyme, Asp2 or memapsin 2 (BACE-1) leads to increased β-secretase activity while displaying appropriate cleavage site specificity for APP. The N-glycosylation and phosphorylation of BACE-1 within its C-terminal domain regulated its intracellular trafficking.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
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