β-site APP cleaving enzyme (BACE-1) is known as β-secretase. It consists of an N-terminal signal peptide (SP), a pro-peptide (Pro) domain, a catalytic domain, a transmembrane domain and a C-terminal tail.
BACE1, 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.
Immunogen
Synthetic peptide directed towards the N terminal region of human BACE1
Biochem/physiol Actions
β-site APP cleaving enzyme (BACE-1) acts as a rate-limiting enzyme of amyloid-β-peptide (Aβ). Overexpression of BACE-1 leads to increased β-secretase activity.
Sequence
Synthetic peptide located within the following region: GQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTY
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The amyloid cascade hypothesis proposes that excessive accumulation of amyloid beta-peptides is the initiating event in Alzheimer's disease. These neurotoxic peptides are generated from the amyloid precursor protein via sequential cleavage by β- and γ-secretases in the 'amyloidogenic' proteolytic pathway.
beta-Site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways
Journal of advanced research, 35, 231-243 (2022-01-14)
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