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Structure of [beta]-Amyloid (12-28)
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Neuroscience

[beta]-Amyloid (12-28) VHHQKLVFFAEDVGSNK

Product number: EP10025_1

€105.00*

Prices excl. VAT plus shipping costs
Available, delivery time: 3 weeks
sterile and endotoxin free
Delivery Format: The product is supplied freeze dried.
Purity: 95% HPLC-MS
Caution: For research use only. Not for use in humans.
Amount in mg
1
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Description

Aβ (12-28) represents a binding site for apolipoprotein E (apoE). ApoE is a genetically inherited risk factor for Alzheimer’s disease that promotes aggregation of toxic Aβ. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Aß (11-28) and five other fragments enhanced aggregation of full length Aß (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length Aß.

TechData

Sequence: VHHQKLVFFAEDVGSNK
Gene: APP
Delivery: 3 weeks
C-Terminus: OH
N-Terminus: H
Amount: 1 mg
Counterion: TFA
Protein: Amyloid-beta precursor protein
UniProt Id: P05067
IEDB Id: 105021
Species: Human
Application: ELISPOT, Flow Cytometry, Western Blotting
Indication: Neuroscience
Purity: 95% HPLC-MS

Documents

Material data sheet Safety data sheet Storage and handling of peptides Probing of membranes with HRP
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