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AnaSpec Offers Beta-Amyloid (1-40) and (1-42) Peptides

Published: Tuesday, December 04, 2012
Last Updated: Tuesday, December 04, 2012
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HFIP treated peptides for the advancement of Alzheimer’s disease research.

AnaSpec, EGT Group has provided a whole suite of reagents for the advancement of Alzheimer’s disease (AD) research.

From peptides to assay kits to antibodies to dyes, AnaSpec is the trusted source of integrated proteomics solutions for AD research.

Amongst the more than 300 β-amyloid peptides, we offer β-amyloid (1-40) and (1-42) that are HFIP treated.

β-amyloids are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 40-42), the latter corresponding to a part of the transmembrane domain of APP.

β-Amyloid assembly into fibrils is initiated by a conformational transition from random coil to β-sheet (hence the name β-amyloid) and a nucleation-dependent aggregation process.

Aβ peptides that are 39 to 42 amino acid residues in length with a molecular mass of approximately 4 kDa are the core components of neuritic plaques seen in Alzheimer’s disease (AD) brains.

Studies have found that dissolving in HFIP favors alpha helical structure and tends to be monomeric.

HFIP treatment of lyophilized Aβ-peptide results in a dense, homogeneous preparation of unaggregated peptide and samples can be stored as peptide films.


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