Beta-Amyloid (1-42), FAM-labeled
- Cat.Number : AS-23526-01
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Aß (1-42), a major component of amyloid plaques, accumulates in neurons of Alzheimer’s disease brains. Biochemical analysis of the amyloid peptides isolated from Alzheimer’s disease brain indicates that Aß (1-42) is the principal species associated with senile plaque amyloids, while Aß (1-40) is more abundant in cerebrovascular amyloid deposit. This is a fluorescent (FAM)-labeled ß-Amyloid peptide, Abs/Em=494/521 nm.
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Citations
Macrophage-Mediated Degradation of β-Amyloid via an Apolipoprotein E Isoform-Dependent Mechanism
J Neurosci . 2009 Mar 18 ; 29(11) 3603 | DOI : https://doi.org/10.1523/JNEUROSCI.5302-08.2009
- L. Zhao
Distinct modulation of microglial amyloid β phagocytosis and migration by neuropeptides (i).
J Neuroinflammation. . 2010 Oct 11 ; 7 61 | DOI : 10.1186/1742-2094-7-61
- S. Fleisher-Berkovich
Preferential accumulation of Aβ(1−42) on gel phase domains of lipid bilayers: An AFM and fluorescence study
Biochim Biophys Acta. . 2007 Jan 01 ; 1768(1) 146 | DOI : 10.1016/j.bbamem.2006.09.005
- A. Choucair
Internalization of β-amyloid peptide by primary neurons in the absence of apolipoprotein E
J Biol Chem. . 2007 Dec 07 ; 282(49) 35722 | DOI : 10.1074/jbc.M701823200
- L. Saavedra
Alzheimer's β-peptide oligomer formation at physiologic concentrations
Anal Biochem. . 2004 Dec 01 ; 335(1) 81 | DOI : 10.1016/j.ab.2004.08.014
- H. LeVine
References
β-Amyloid peptide-induced death of PC 12 cells and cerebellar granule cell neurons is inhibited by long-term lithium treatment
Eur. J. Pharmacol. . 2000 Mar 31 ; 392(3) 117 | DOI : https://doi.org/10.1016/S0014-2999(00)00127-8
- H. Wei
- et al