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Beta - Amyloid (12 - 28)
| Overview | |
|---|---|
| Description | Aß (12 €“28) residues are the binding site for apolipoprotein E (apoE) on Aß. 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. |
| Sequence | VHHQKLVFFAEDVGSNK |
| Sequence (3 Letter) | H-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-OH |
| Molecular Weight | 1955.2 |
| Properties | |
| Purity | > 95% By HPLC |
| Storage | Store at -20 °C, cap vial tightly at all times. |
Sadowski, M. et al. Am. J. Pathol. 165, 937 (2004); Liu, R. et al. J. Neurosci. Res. 75, 162 (2004).
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