S9564
Amyloid Precursor Protein α, Secreted human
>90% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), buffered aqueous solution
Sinónimos:
sAPPα
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25 μG
MXP 12,979.00
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25 μG
MXP 12,979.00
About This Item
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Descripción general
Aplicación
Acciones bioquímicas o fisiológicas
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.[6]
Forma física
Solution 0.2 μm filtered, in phosphate buffered saline, pH 7.4.
Nota de preparación
Expressed as a soluble protein and purified under non-denaturing conditions.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
nwg
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°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)
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
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
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