β-Secretaseis an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths in peripheral nerve cells. The transmembrane protein, contains two active site aspartate residues in its extracellular protein domain and may function as a dimer.Generation of the 40 or 42 amino acid-long amyloid-β peptides that aggregate in the brain of Alzheimer's patients requires two sequential cleavages of the amyloid precursor protein (APP). Extracellular cleavage of APP by BACE releases a soluble extracellular fragment and is followed by APP cleavage within its transmembrane domain by γ-secretase. The second cleavage releases the intracellular domain of APP and amyloid-β. Since alpha-secretase cleaves APP closer to the cell membrane than BACE does.
Human Beta-site APP-Cleaving Enzyme 1 (BACE1) ELISA Kit employs a two-site sandwich ELISA to quantitate BACE1 in samples. An antibody specific for BACE1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyBACE1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for BACE1 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of BACE1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Human Beta-site APP-Cleaving Enzyme 1 (BACE1) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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