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| Amyloid Peptides - The World's Most Comprehensive Collection |
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Amyloid Peptides
AnaSpec has been providing ß-Amyloid peptides to leading Alzheimer’s researchers for almost 10 years. As interest in amyloid peptides continues to grow, AnaSpec has developed an extensive selection of catalog amyloid peptides to match that interest. Optimally equipped with expertise in both peptide synthesis and detection technologies, AnaSpec is proud to offer the world’s most comprehensive collection of amyloid peptides.
ß-Amyloid (Aß) peptides, made up of long, insoluble ordered fibers, are glycoproteins deposited extracellularly in tissues in amyloidosis. These peptides are generated as cleavage products from the membrane protein, Amyloid Precursor Protein (APP) by two proteases, ß-secretase and γ-secretase. Aßs are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 40), the latter corresponding to a part of the transmembrane domain of APP. These insoluble amyloid deposits found in Alzheimer’s diseased brains have been the subject of increased interest for Alzheimer’s treatment (reviewed in 1, 2).
Our comprehensive collection includes:
Aßs of various lengths
Amino acid-substituted Aßs
Dye-labeled Aßs
Biotin-labeled Aßs
Sodium forms
HCl forms
TFA salt forms(Standard form, unless otherwise specified)
iAb5p and other-Aß inhibitors
Humanins
Secretase fluorescent resonance energy transfer (FRET) substrates and inhibitors
For a complete listing of AnaSpec's amyloid peptides, click here.
References:
1. Selkoe DJ. Nature 399, A23 (1999).
2. Suh, Y-H. and F. Checler. Pharma. Rev. 54, 469 (2002).
3. Suzuki, N. et al. Science 264, 1336 (1994).
4. Iwatsubo, T. et al. Neuron 13, 45 (1994).
5. Citron, M. et al. Nature (London) 360, 672 (1992).
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