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Merck
CN

SCP0053

Sigma-Aldrich

[Glu11]-Amyloid β 1-28 human

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关于此项目

经验公式(希尔记法):
C145H209N41O46
分子量:
3262.46
UNSPSC代码:
12352209
NACRES:
NA.32
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方案

≥95% (HPLC)

表单

lyophilized

组成

Peptide Content, ≥70%

储存条件

protect from light

储存温度

−20°C

Amino Acid Sequence

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

应用

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.

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

新产品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Daniela Valensin et al.
Inorganic chemistry, 49(11), 4720-4722 (2010-05-13)
The reaction of the ruthenium(II) complex fac-[Ru(CO)(3)Cl(2)(N(1)-thz)] (I hereafter; thz = 1,3-thiazole) with human beta-amyloid peptide 1-28 (Abeta(28)) and the resulting {Ru(CO)(3)}(2+) peptide adduct was investigated by a variety of biophysical methods. (1)H NMR titrations highlighted a selective interaction of
Phosphorus Dendrimers Affect Alzheimer's (Aμ(1-28)) Peptide and MAP-Tau Protein Aggregation.
Wasiak T, Ionov M, Nieznanski K, et al.
Molecular Pharmacology, 9(3), 458-469 (2012)
Daniela Valensin et al.
Inorganic chemistry, 50(15), 6865-6867 (2011-07-02)
The reactions of human β-amyloid peptide 1-28 (Aβ28) with Al(III) and Fe(III) ions were investigated by (1)H NMR and electrospray ionization mass spectrometry (ESI-MS) under pH conditions close to physiological ones. (1)H NMR titrations, performed in the 5.3-8.0 pH range

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