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S9564

Sigma-Aldrich

Amyloid Precursor Protein α, Secreted human

>90% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), buffered aqueous solution

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Synonym(s):
sAPPα
MDL number:
NACRES:
NA.32

recombinant

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

Quality Level

assay

>90% (SDS-PAGE)

form

buffered aqueous solution

mol wt

~100 kDa by SDS-PAGE

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... APP(351)

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This Item
A2201A9810MABN2273
vibrant-m

A2201

Amyloid β-Protein Fragment 35-25

vibrant-m

A9810

Amyloid β Protein Fragment 1-42

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

100

assay

>90% (SDS-PAGE)

assay

≥95% (HPLC)

assay

≥95% (HPLC)

assay

-

form

buffered aqueous solution

form

powder

form

powder

form

-

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

ambient

mol wt

~100 kDa by SDS-PAGE

mol wt

-

mol wt

-

mol wt

-

General description

The APP (amyloid precursor protein) gene is mapped to human chromosome 21q21.3. It encodes a integral membrane protein. APPα is a soluble protein generated by sequential cleavage with α and γ secretase.

Application

Human amyloid precursor protein α secreted, has been used in enzyme linked immunosorbent assay (ELISA).

Biochem/physiol Actions

Amyloid precursor protein α is an α-secretase-cleaved soluble protein that has been shown to have neuroprotective properties. It is derived from amyloid precursor protein. The protein consists of 612 amino acids. Several G protein-coupled receptors are known to activate α-secretase-dependent processing of APP. It has neuroprotective, neurogenic and neurotrophic functions. Amyloid precursor protein a also stimulates gene expression and protein expression.

Physical form

Solution 0.2 μm filtered, in phosphate buffered saline, pH 7.4.

Preparation Note

Expressed as a soluble protein and purified under non-denaturing conditions.

Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Luo, J.J., et al.
Neuroscience Research, 63, 410-410 (2001)
In vivo BACE1 inhibition leads to brain A?
lowering and increased a-secretase processing of
APP without effect on Neuregulin-1
Sethu Sankaranarayanan
American Society for Engineering Education (2018)
S W Barger et al.
Journal of neurochemistry, 76(3), 846-854 (2001-02-07)
Microglial activation as part of a chronic inflammatory response is a prominent component of Alzheimer's disease. Secreted forms of the beta-amyloid precursor protein (sAPP) previously were found to activate microglia, elevating their neurotoxic potential. To explore neurotoxic mechanisms, we analyzed
Dementia: New Insights for the Healthcare Professional, 478-478 (2013)
S W Barger et al.
Brain research. Molecular brain research, 40(1), 116-126 (1996-08-01)
A significant fraction of the beta-amyloid precursor protein is proteolytically processed to yield large secreted forms (sAPP). These proteins have pleiotropic effects which potentially involve control of gene expression. We have investigated the influence of sAPP on the class of

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