AG968
β Amyloid 1-42, aβ, ultra pure, HFIP, recombinant human
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About This Item
UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.41
Productos recomendados
biological source
human
Quality Level
assay
>97.0%
form
powder
manufacturer/tradename
Chemicon®
NCBI accession no.
UniProt accession no.
Gene Information
human ... APP(351)
General description
β Amyloid 1-42 is a derivative of integral membrane-bound amyloid precursor protein. It is the most important alloform of the Alzheimer′s peptide.
Application
β Amyloid 1-42, aβ, ultra-pure, HFIP, recombinant human has been used:
- to study its effect on the activity of mitochondrial BKCa (mitoBKCa) channels in human astrocytoma cells through patch-clamp technique
- to study its effect on alteration in protein levels of dystrophic neurites (DNs) forming proteins in mouse neuroblastoma cells
- to induce Alzheimer′s disease in a rat model for experimental studies
Biochem/physiol Actions
β Amyloid 1-42 causes neurotoxicity and is implicated in the pathogenesis of Alzheimer′s disease (AD). β Amyloid (βA) acts as a ligand for several receptors and other molecules involved in complex trafficking pathways in tissues and blood-brain barriers. βA along with amylin elevates cyclic adenosine monophosphate (cAMP) and Ca2+ in turn activates multiple signaling pathway mediators like mitogen-activated protein kinase (MAPK), protein kinase A/B, and cFOS. It acts as the main source of AD-associated neuroinflammation.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Stephanie J Soscia et al.
PloS one, 5(3), e9505-e9505 (2010-03-09)
The amyloid beta-protein (Abeta) is believed to be the key mediator of Alzheimer's disease (AD) pathology. Abeta is most often characterized as an incidental catabolic byproduct that lacks a normal physiological role. However, Abeta has been shown to be a
Annika Olsson et al.
Clinical chemistry, 51(2), 336-345 (2004-11-26)
To simultaneously study several biomarkers for Alzheimer disease (AD), we used the xMAP technology to develop and evaluate a multiparametric bead-based assay for quantification of beta-amyloid((1-42)) [Abeta((1-42))], total tau (T-TAU), and hyperphosphorylated tau [P-TAU((181P))] in cerebrospinal fluid (CSF). We compared
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