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S8065

Sigma-Aldrich

Amyloid Precursor Protein α (304-612), Secreted human

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

Synonym(s):

sAPPα (304-612)

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About This Item

MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32

recombinant

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

assay

>90% (SDS-PAGE)

form

buffered aqueous solution

mol wt

apparent mol wt ~45 kDa by SDS-PAGE

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... APP(351)

Biochem/physiol Actions

Secreted Amyloid Precursor Protein α (sAPPα) is a 612 amino acid protein produced from the ubiquitously expressed β-Amyloid precursor protein (βAPP), 695 isoform, by α-secretase cleavage. sAPPα (304-612) is a fragment of sAPPα designed to lack the N-terminal domain of the full length protein.

Physical form

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

Preparation Note

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

Certificates of Analysis (COA)

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Mattson, M.P.
The Journal of Neuroscience, 25, 439-439 (1994)
Greenfield, J.P.,
Frontiers in Bioscience, 5, 72-72 (2000)
S W Barger et al.
Nature, 388(6645), 878-881 (1997-08-28)
A role for beta-amyloid precursor protein (beta-APP) in the development of Alzheimer's disease has been indicated by genetics, and many conditions in which beta-APP is raised have been associated with an increased risk of Alzheimer's disease or an Alzheimer's-like pathology.
L W Jin et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 14(9), 5461-5470 (1994-09-01)
Amyloid beta/A4 protein precursor (APP) is secreted into medium by most cultured cells and can function as an autocrine factor. To study the biological function of secreted forms of APP (sAPP) on neurons, we used a clonal CNS neuronal line
D H Small et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 14(4), 2117-2127 (1994-04-01)
The amyloid protein precursor (APP) of Alzheimer's disease is synthesized as an integral transmembrane protein that is released from cells in culture following proteolytic cleavage. The function of released APP is not known, although there is evidence that the protein

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