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
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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Regulation of global gene expression and cell proliferation by APP.
Wu Y
Scientific Reports (2016)
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)
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
C Haass et al.
Nature, 357(6378), 500-503 (1992-06-11)
Progressive cerebral deposition of the amyloid beta-peptide is an early and invariant feature of Alzheimer's disease. The beta-peptide is released by proteolytic cleavages from the beta-amyloid precursor protein (beta APP), a membrane-spanning glycoprotein expressed in most mammalian cells. Normal secretion
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