|Calculated MW||55711 Da|
|Positive Control||Western blot: Recombinant protein|
|Application & Usage||Western blot: ~1:200|
|Other Names||ASP2, BACE, HSPC104, KIAA1149, Beta-secretase-1, memapsin-2, aspartyl-protease-2, beta-site-APP-cleaving-enzyme-1|
|Formulation||100 µg or 30 µg (0.5 mg/ml) of antibody in PBS pH 7.2 containing 0.01 % BSA, 0.01 % thimerosal, and 50 % glycerol.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||BACE1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface|
|Tissue Location||Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata|
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Provided below are standard protocols that you may find useful for product applications.
Beta-secretase 1 (BACE1) also known as beta-site APP cleaving enzyme 1 (beta-site amyloid precursor protein cleaving enzyme 1), memapsin-2 (membrane-associated aspartic protease 2), and aspartyl protease 2 (ASP2), β-Secretase, and is a member of the peptidase A1 protein family, BACE1 is a type I integral membrane glycoprotein and aspartic protease that is found mainly in the Golgi. BACE1 is 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. This protease is responsible for the proteolytic processing of the amyloid precursor protein (APP). 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 APP. Extracellular cleavage of APP by BACE creates a soluble extracellular fragment and a cell membrane-bound fragment referred to as C99. The elevation of BACE1 levels can be induced by amyloid plaques surrounding neurons at early stages of pathology before neuron death occurs, and may drive a positive-feedback loop in AD.
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