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S4316

Sigma-Aldrich

Amyloid Precursor Protein β, Secreted human

recombinant, expressed in E. coli (N-terminal histidine tagged), solution

Synonyme(s) :

Amyloid Precursor Protein β, Secreted, sAPPβ

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About This Item

Numéro MDL:
MFCD06201921
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli (N-terminal histidine tagged)

Niveau de qualité

200

Forme

solution

Poids mol.

~100 kDa by SDS-PAGE

Numéro d'accès UniProt

P05067

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... APP(351)

Description générale

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Notes préparatoires

sAPPβ was expressed in E. coli as a soluble protein and purified under non-denaturing conditions

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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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
The Processing of Amyloid Precursor Protein in the
Central Nervous System of Humans and Rhesus
Macaques
Justyna Anna Dobrowolska
The West Virginia Medical Journal (2013)
Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering.
Zhang-Haagen B
PLoS ONE (2016)
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
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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Alzheimer's Disease and its Biochemical Pathways

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