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Key Documents

SCP0033

Sigma-Aldrich

Amyloid β 1-16 rat

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About This Item

Fórmula empírica (notación de Hill):
C80H115N25O27
Peso molecular:
1858.92
UNSPSC Code:
12352200
NACRES:
NA.32

assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥75%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Asp-Ala-Glu-Phe-Gly-His-Asp-Ser-Gly-Phe-Glu-Val-Arg-His-Gln-Lys

Application

Amyloid β (Aβ) refers to peptides derived from Amyloid precursor protein that vary in length from 36-43 amino acids. Aβ(s) peptides, their peptide fragments and mutated fragments are used to study a wide range of metabolic and regulatory functions including activation of kinases, regulation of cholesterol transport, function as a transcription factor, and regulators of inflammation. Aβ(s) peptides and their peptide fragments are also used to study oxidative stress, metal binding and mechanisms of protein cross-linking in the context of diseases such as Alzheimer′s disease and neurodegeneration.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Lian Hong et al.
The journal of physical chemistry. B, 114(34), 11261-11271 (2010-08-10)
There is no consensus on the coordinating ligands for Cu(2+) by Abeta. However, the differences in peptide sequence between human and rat have been hypothesized to alter metal ion binding in a manner that alters Cu(2+)-induced aggregation of Abeta. Herein
Maryam Bagheri et al.
Neurobiology of learning and memory, 95(3), 270-276 (2010-12-15)
Alzheimer's disease (AD) is a debilitating neurodegenerative disorder characterized by increased β-amyloid (Aβ) deposition and neuronal dysfunction leading to impaired learning and recall. Ageing, heredity, and induced oxidative stress are among proposed risk factors. The increased frequency of the disease
Yan Wang et al.
Neuropharmacology, 62(2), 871-881 (2011-10-01)
Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by the accumulation of β-sheet-rich amyloid oligomers or fibrils which are associated with cellular toxicity in the brain. Inhibition of Aβ aggregation could be a viable therapeutic strategy for slowing and/or
Aynun N Begum et al.
Journal of Alzheimer's disease : JAD, 15(4), 625-640 (2008-12-20)
The rat amyloid-beta (Abeta) intracerebroventricular infusion can model aspects of Alzheimer's disease (AD) and has predicted efficacy of therapies such as ibuprofen and curcumin in transgenic mouse models. High density lipoprotein (HDL), a normal plasma carrier of Abeta, is used
Tania Araujo Viel et al.
Neurobiology of aging, 29(12), 1805-1814 (2007-06-16)
Although numerous inflammation pathways have been implicated in Alzheimer's disease, the involvement of the kallikrein-kinin system is still under investigation. We anatomically localized and quantified the density of kinin B(1) and B(2) receptors binding sites in the rat brain after

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