We use cookies to offer you the best experience on our site. You can find out more about the cookies we use or disable them in the Cookie settings
Beta-Amyloid (1-42), FAM-labeled
- Cat.Number : AS-23526-01
- Manufacturer Ref. :
-
Availability :
In stock
Alternative choices
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.
Specifications
Chemistry | |
Sequence one letter code |
|
---|---|
Sequence three letter code |
|
CAS registry number |
|
Molecular Formula |
|
Molecular Mass/ Weight |
|
Properties | |
Absorbance (nm) |
|
Emission (nm) |
|
Modification | |
Conjugation type |
|
Modification Name | |
Conjugation |
|
Quantity & Purity | |
Purity |
|
Storage & stability | |
Form |
|
Activity | |
Biomarker Target | |
Detection Method | |
Research Area | |
Sub-category Research Area | |
Usage |
|
Source | |
Source / Species |
|
Codes | |
Code Nacres |
|
Downloads
You may also be interested in the following product(s)
Citations
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
- et al
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
- et al
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
- et al
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
- et al