beta-Amyloid (12-28)

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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.

Clear
Catolog No: N/A Category:

Sequence (One-Letter Code):

VHHQKLVFFAEDVGSNK

 

Sequence (Three-Letter Code):

{Val}{His}{His}{Gln}{Lys}{Leu}{Val}{Phe}{Phe}{Ala}{Glu}{Asp}{Val}{Gly}{Ser}{Asn}{Lys}

 

Molecular Weight:

1955.2

 

Purity:
% Peak Area By HPLC ≥ 95%

 

Salt:
TFA Salt

 

Storage:

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

 

Note:

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.

 

Documents:

MSDS

Amount

0.5 mg, 1 mg, Other