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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:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Produit recombinant

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

Niveau de qualité

Forme

solution

Poids mol.

~100 kDa by SDS-PAGE

Numéro d'accès UniProt

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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Consulter la Bibliothèque de documents

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
Regulation of global gene expression and cell proliferation by APP.
Wu Y
Scientific Reports (2016)
Conformational Dynamics of Specific A? Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis.
Dean DN
Biochemistry (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)
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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