S9564
Amyloid Precursor Protein α, Secreted human
>90% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), buffered aqueous solution
Synonyme(s) :
sAPPα
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Description générale
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).
Actions biochimiques/physiologiques
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.
Forme physique
Solution 0.2 μm filtered, in phosphate buffered saline, pH 7.4.
Notes préparatoires
Expressed 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)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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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)
Therapeutic Potential of Secreted Amyloid Precursor Protein APPsa
Frontiers in Molecular Neuroscience (2017)
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
Soluble ?-amyloid Precursor Protein Alpha Binds to p75 Neurotrophin Receptor to Promote Neurite Outgrowth
Noriko Hasebe
PLoS ONE (2013)
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