Human CellExp™ BACE1, human recombinant (Native)

Involved in proteolytic processing of APP and pathogenesis of Alzheimer's disease
Catalog #: 7398 | abID:

Product Details

Alternate Name BACE1, ASP2, BACE, FLJ90568, HSPC104, KIAA1149, Beta-secretase-1, memapsin-2, aspartyl-protease-2, beta-site-APP-cleaving-enzyme-1
Gene Symbol BACE1
Gene ID 23621
Accession # P56817
Source HEK293 cells
Appearance Lyophilized
Physical Form Description Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Molecular Weight This protein contains no “tags” and has a calculated MW of 49 kDa. The predicted N-terminus is Thr22. DTT-reduced protein migrates as 50-65 kDa polypeptide in SDS-PAGE due to glycosylation.
Purity by SDS-PAGE ≥98%
Endotoxin Level <1 EU/μg by LAL method
Biological Activity Measured by its ability to cleave a fluorescent peptide substrate Mca-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Arg-Lys(Dnp)-Arg-Arg-NH2. Cleavage of the substrate can be measured using excitation and emission wavelengths of 320 and 405 nm, respectively. The sp
Reconstitution Instructions Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans

Details

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.[1] 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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