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Merck
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Principaux documents

SCP0040

Sigma-Aldrich

Amyloid β 17-42 human

≥80% (HPLC)

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About This Item

Formule empirique (notation de Hill):
C119H194N28O33S1
Poids moléculaire :
2577.05
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Essai

≥80% (HPLC)

Forme

lyophilized

Composition

Peptide Content, ≥80%

Conditions de stockage

protect from light

Température de stockage

−20°C

Amino Acid Sequence

Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
MD0606

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Wanli Wei et al.
Brain : a journal of neurology, 125(Pt 9), 2036-2043 (2002-08-17)
The p3 peptide [amyloid beta-peptide (Abeta) 17-40/42], derived by alpha- and gamma-secretase cleavage of the amyloid precursor protein (APP), is a major constituent of diffuse plaques in Alzheimer's disease and cerebellar pre-amyloid in Down's syndrome. However, the importance of p3
Yifat Miller et al.
Biophysical journal, 97(4), 1168-1177 (2009-08-19)
Abeta(17-42) (so-called p3) amyloid is detected in vivo in the brains of individuals with Alzheimer's disease or Down's syndrome. We investigated the polymorphism of Abeta(17-42) oligomers based on experimental data from steady-state NMR measurements, electron microscopy, two-dimensional hydrogen exchange, and
Jie Zheng et al.
The journal of physical chemistry. B, 112(22), 6856-6865 (2008-05-07)
We report all-atom molecular dynamics simulations of annular beta-amyloid (17-42) structures, single- and double-layered, in solution. We assess the structural stability and association force of Abeta annular oligomers associated through different interfaces, with a mutated sequence (M35A), and with the
Nikolay Blinov et al.
Biophysical journal, 98(2), 282-296 (2010-03-27)
Amyloid fibrils are associated with many neurodegenerative diseases. It was found that amyloidogenic oligomers, not mature fibrils, are neurotoxic agents related to these diseases. Molecular mechanisms of infectivity, pathways of aggregation, and molecular structure of these oligomers remain elusive. Here

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