HEK293 Cells.
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Filtered clear solution.
Greater than 95.0% as determined by SDS-PAGE.
BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa.
BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
HEK293 Cells.
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
BACE2 is a type I integral membrane glycoprotein and aspartic protease. The mouse recombinant version of BACE2 produced in HEK293 cells is a single, glycosylated polypeptide chain consisting of 449 amino acids, with a molecular mass of approximately 48.6 kDa . This recombinant protein is often tagged with a His-tag at the C-terminus to facilitate purification .
BACE2 cleaves APP at specific sites, contributing to the formation of amyloid-beta peptides. These peptides aggregate to form amyloid plaques, which are a hallmark of Alzheimer’s disease . BACE2 is also involved in the processing of other proteins, such as Pmel17 in melanocytes, where it mediates the release of the amyloidogenic ectodomain .
In addition to its role in amyloid-beta production, BACE2 has been shown to prevent neuronal apoptosis by cleaving a potassium channel at the plasma membrane . This dual functionality highlights the enzyme’s complex role in cellular processes and its potential impact on neurodegenerative diseases.
The regulation of BACE2 is less studied compared to BACE1. However, it is known that BACE2 degradation is mediated by both the proteasome and lysosome pathways. Inhibition of these pathways leads to an increase in BACE2 levels in both neuronal and non-neuronal cells . This suggests that dysregulation of BACE2 could be linked to the pathogenesis of Alzheimer’s disease.
Recombinant BACE2 produced in HEK293 cells is widely used in research to study its structure, function, and role in disease. Understanding the mechanisms of BACE2 activity and regulation can provide insights into potential therapeutic targets for Alzheimer’s disease and other neurodegenerative conditions.