This protein carries no "tag". The protein has a calculated MW of 49 kDa. The protein migrates as 60-70 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
BACE1
Spezies: Maus
Wirt: Escherichia coli (E. coli)
Recombinant
> 95 %
WB, SDS, Imm, PC
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
50 mM Tris, pH 8.0
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Mycroft-West, Devlin, Cooper, Procter, Miller, Fernig, Guerrini, Guimond, Lima, Yates, Skidmore: "Inhibition of BACE1, the β-secretase implicated in Alzheimer's disease, by a chondroitin sulfate extract from Sardina pilchardus." in: Neural regeneration research, Vol. 15, Issue 8, pp. 1546-1553, (2020) (PubMed).
Peters-Libeu, Campagna, Mitsumori, Poksay, Spilman, Sabogal, Bredesen, John: "sAβPPα is a Potent Endogenous Inhibitor of BACE1." in: Journal of Alzheimer's disease : JAD, Vol. 47, Issue 3, pp. 545-55, (2015) (PubMed).
Beta-secretase 1 (BACE1) is 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.