S9564
Amyloid Precursor Protein α, Secreted human
>90% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), buffered aqueous solution
Synonym(s):
sAPPα
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About This Item
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.
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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In vivo BACE1 inhibition leads to brain A?
lowering and increased a-secretase processing of
APP without effect on Neuregulin-1
lowering and increased a-secretase processing of
APP without effect on Neuregulin-1
Sethu Sankaranarayanan
American Society for Engineering Education (2018)
Luo, J.J., et al.
Neuroscience Research, 63, 410-410 (2001)
Dementia: New Insights for the Healthcare Professional, 478-478 (2013)
Soluble ?-amyloid Precursor Protein Alpha Binds to p75 Neurotrophin Receptor to Promote Neurite Outgrowth
Noriko Hasebe
PLoS ONE (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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