Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
BACE1, also known as beta-secretase 1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein encoded by the BACE1 gene in humans. This protein is primarily found in neurons and plays a vital role in myelin sheath formation in the peripheral nervous system. BACE1 is a transmembrane protein, meaning it is embedded within the cell membrane. It functions as a dimer, with two active sites (aspartate residues) located in its extracellular domain.
This product consists of human BACE1, produced in Sf9 insect cells using a baculovirus expression system. It is a single, glycosylated polypeptide chain with a molecular weight of 49.2 kDa. The recombinant protein encompasses amino acids 22-457 and includes a 6-amino acid His tag at the C-terminus. Purification is achieved through proprietary chromatographic methods.
The BACE1 protein is supplied in a solution of Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
For optimal storage, keep the vial at 4°C if using within 2-4 weeks. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing of the product.
The specific activity is greater than 5 pmol/min/µg. One unit of activity is defined as the amount of enzyme required to convert 1.0 picomole of the substrate Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA-Pro-Leu-OH per minute at a pH of 3.5 and temperature of 25°C.
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH HH.
BACE1 is a type I membrane protein with a single transmembrane domain. It is synthesized as a precursor protein and undergoes post-translational modifications, including glycosylation and proteolytic cleavage, to become fully active . The enzyme cleaves the amyloid precursor protein (APP) at the β-site, producing a soluble APP fragment and a membrane-bound C-terminal fragment (C99). The C99 fragment is subsequently cleaved by γ-secretase to generate Aβ peptides .
The accumulation of Aβ peptides in the brain is a hallmark of Alzheimer’s disease. These peptides aggregate to form amyloid plaques, which are believed to disrupt cell function and trigger neurodegenerative processes . Genetic mutations in APP or presenilin genes (components of γ-secretase) can increase the production of Aβ, leading to early-onset familial Alzheimer’s disease .
Given its critical role in Aβ production, BACE1 has been a major target for drug development aimed at reducing Aβ levels in the brain. Inhibitors of BACE1 are being investigated as potential treatments for Alzheimer’s disease. However, developing effective BACE1 inhibitors has been challenging due to the enzyme’s broad substrate specificity and the need to avoid off-target effects .
Recombinant BACE1 is produced using various expression systems, including insect cells and mammalian cells like HEK 293 . These recombinant proteins are used in research to study the enzyme’s structure, function, and interactions with potential inhibitors. They are also employed in high-throughput screening assays to identify new BACE1 inhibitors .