S4316
Amyloid Precursor Protein β, Secreted human
recombinant, expressed in E. coli (N-terminal histidine tagged), solution
Synonym(s):
Amyloid Precursor Protein β, Secreted, sAPPβ
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General description
Amyloid-β (Aβ) peptides are a major component of the senile plaques characteristic of the Alzheimer brain. It is a type- I transmembrane protein. The gene encoding amyloid-β is localized on human chromosome 21.
Application
Human amyloid precursor protein β has been used as peptide standard.
Biochem/physiol Actions
The secreted amyloid precursor β (sAPPβ) is a proteolytic cleavage product of β amyloid precursor protein (APP). APP is cleaved by β-secretase into two fragments, sAPPβ and β-amyloid peptide (Aβ). The Aβ is a component of amyloid plaques, one of the major hallmarks of Alzheimer`s disease (AD), while the sAPPβ is thought to modulate neuronal function and cell survival. Mutation in APP found in Swedish familial AD pedigree increases the susceptibility of APP to β-secretase cleavage and the formation of Aβ and sAPPβ. In contrast, activation of protein kinase C (PKC) decreases the levels of sAPPβ. The trans-Golgi network (TGN) is the major site for β-secretase activity.
Physical form
0.2 μm filtered solution in 20 mM Tris (pH 7.4), 0.5 M NaCl, 1 mM EDTA, 5 mM βME, 2 μg/ml aprotinin
Preparation Note
sAPPβ was expressed in E. coli as a soluble protein and purified under non-denaturing conditions
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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D J Selkoe
Nature, 399(6738 Suppl), A23-A31 (1999-07-07)
Studies of the molecular basis of Alzheimer's disease exemplify the increasingly blurred distinction between basic and applied biomedical research. The four genes so far implicated in familial Alzheimer's disease have each been shown to elevate brain levels of the self-aggregating
In vivo BACE1 inhibition leads to brain A? lowering and increased a-secretase processing of APP without effect on Neuregulin-1
Sethu Sankaranarayanan
Journal of Pharmacology and Experimental Therapeutics (2018)
Conformational Dynamics of Specific A? Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis.
Dean DN
Biochemistry (2016)
Regulation of global gene expression and cell proliferation by APP.
Wu Y
Scientific Reports (2016)
D M Skovronsky et al.
The Journal of biological chemistry, 275(4), 2568-2575 (2000-01-25)
The release of amyloidogenic amyloid-beta peptide (Abeta) from amyloid-beta precursor protein (APP) requires cleavage by beta- and gamma-secretases. In contrast, alpha-secretase cleaves APP within the Abeta sequence and precludes amyloidogenesis. Regulated and unregulated alpha-secretase activities have been reported, and the
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