SCP0034
Amyloid β 12-28 human
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500 μG
118,00 €
1 MG
214,00 €
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500 μG
118,00 €
1 MG
214,00 €
About This Item
Empirische Formel (Hill-System):
C89H135N25O25
Molekulargewicht:
1955.18
UNSPSC-Code:
12352200
NACRES:
NA.32
Assay
≥95% (HPLC)
Form
lyophilized
Zusammensetzung
Peptide Content, ≥70%
Lagerbedingungen
protect from light
Lagertemp.
−20°C
Amino Acid Sequence
Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys
Anwendung
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.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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Samaneh Beheshti et al.
Chemphyschem : a European journal of chemical physics and physical chemistry, 13(2), 542-548 (2011-12-14)
The synthesis and characterization of four new Ferrocene (Fc) bioconjugates, bearing a podant (Lys)-Leu-Val-Phe-Phe motif, namely the hydrophobic sequence of amyloid-β-peptides (Aβ), is reported. The Fc-peptide conjugates are characterized by a reversible redox activity and the ability to undergo hydrophobic
Zanxia Cao et al.
International journal of molecular sciences, 12(11), 8259-8274 (2011-12-17)
The aim of this work is to investigate the effects of different force fields and temperatures on the structural character of Aβ (12-28) peptide in aqueous solution. Moreover, the structural character of Aβ (12-28) peptide is compared with other amyloid
Marino Convertino et al.
The Journal of biological chemistry, 286(48), 41578-41588 (2011-10-05)
In recent years, an increasing number of small molecules and short peptides have been identified that interfere with aggregation and/or oligomerization of the Alzheimer β-amyloid peptide (Aβ). Many of them possess aromatic moieties, suggesting a dominant role for those in
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