Anti-BACE BACE1 Antibody

Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by two proteases. APP is first cleaved by beta-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 gamma-secretase to generate the 4 kDa amyloid-beta peptide, which is deposited in the brains of all suffers of Alzheimer's disease. The long-sought beta-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.

Anti-BACE antibody was raised against a peptide corresponding to 17 amino acids near the carboxy terminus of human BACE. The immunogen is located within the last 50 amino acids of BACE.

Responsible for the proteolytic processing of the amyloid precursor protein (APP) . Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves APP with much more catalytic efficiency than for the wild-type.

BACE antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

WB: 1-4 μg/mL IHC-P: 1-2 μg/mL IHC-P/IF: 10-20 μg/mL. Antibody validated: Western Blot in human and mouse samples; Immunohistochemistry in human samples; Immunofluorescence in mouse samples. All other applications and species not yet tested.