beta-Amyloid (12-28)


Abeta(12-28) residues are the binding site for apolipoprotein E (apoE) on Abeta. This sequence encompasses a hydrophobic domain (residues 14-21) and a beta-turn (residues 22–28) which place two hydrophobic domains of Abeta 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Abeta peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by beta-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 Abeta pathology in Alzheimer’s disease (AD). Beta-amyloid (12-28) and five other fragments enhanced aggregation of full length Abeta (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 Abeta.

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% Peak Area By HPLC ≥ 95%


TFA Salt



Store at -20°C. Store under desiccating conditions. The product can be stored for up to 12 months.



This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.





0.5 mg, 1 mg, Other