Prices plus VAT plus shipping costs
Delivery time 3 weeks
sterile and endotoxin free
Delivery Format: The product is supplied freeze dried.
- Order number: EP10025_1
Injection of the amyloid ?-protein fragment VHHQKLVFFAEDVGSNK into different limbic system structures in mice impaired retention with remarkably similar efficacy and in a dose-dependent manner. A? (12-28) and other A? fragments may exert dysregulatory cognitive effects by incoordination of K? channel function in neurons, glia and endothelial cells. Aï¿½ (12ï¿½28) residues are the binding site for apolipoprotein E (apoE) on Aï¿½. This sequence encompasses a hydrophobic domain (residues 14ï¿½21) and a ï¿½-turn (residues 22ï¿½28) which place two hydrophobic domains of Aï¿½ 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aï¿½ peptides into fibrils. The secondary structure of Aï¿½ (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aï¿½ is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aï¿½ pathology in Alzheimerï¿½s disease (AD). Aï¿½ (11-28) and five other fragments enhanced aggregation of full length Aï¿½ (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 Aï¿½.
|Protein:||Amyloid-beta precursor protein|
|Indication :||Alzheimer's Disease|
Protocols and Tips