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Home > Proteins & Peptides > A-Z Proteins  > BACE1 Protein

BACE1 Protein

β-site APP cleaving enzyme 1, ASP2, HSPC104, Memapsin-2, Aspartyl protease 2, Asp 2, EC 3.4.23.46

Catalog No. Product Name Size List Price (US$) Quantity
BP000751-ENZ-358 Recombinant Human B Site APP-Cleaving Enzyme 1 5 ug 160.00
BP000751-ENZ-358 Recombinant Human B Site APP-Cleaving Enzyme 1 50 ug 1200.00
Description

Introduction
Cerebral deposition of amyloid beta peptide is an early and critical feature of Alzheimer's disease. Amyloid beta peptide is generated by proteolytic cleavage of amyloid precursor protein (APP) by two proteases, one of which is the protein encoded by this gene. BACE1 is a member of the peptidase A1 protein family, is a type I integral membrane glycoprotein and aspartic protease that is found mainly in the Golgi. Four transcript variants encoding different isoforms have been described for this gene. BACE1 is responsible for the proteolytic processing of the amyloid precursor protein (APP). BACE-1 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.

BP000751-ENZ-358: Recombinant Human β Site APP-Cleaving Enzyme 1 (BACE1)

Source: E. coli-derived.
Purity > 95%, by SDS-PAGE.
Formulation: 20 mM Tris, 20 mM KCl, 0.3 M NaCl and 10% glycerol, pH 7.8.
Applications: Recombinant BACE-1 is an excellent protein for proteases functional assays; highly active, excellent for BACE-1 inhibitor screen assay.

Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.

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