Beta-Amyloid (Aß) peptides are generated as cleavage products the Amyloid Precursor Protein (APP) by two proteases, ß-secretase and γ-secretase and are thought to be the causative agent (Shankar et al. Nature Medicine) in Alzheimer’s . Aßs are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 42). The C-terminal domain corresponds to a portion of the transmembrane domain of APP. Heterogeneity at both ends of the peptides is known to affect the toxicity of beta-amyloid peptides. Amyloid deposits are insoluble and the core component of these plaques are Aß peptides that are 39 to 42 amino acid residues in length with a molecular mass of approximately 4 kDa (Olsson et al. Journal of Biological Chemistry). The most common peptide isoforms are Aβ40 and Aβ42 and early-onset Alzheimer’s is correlated with an increased production of Aβ42 relative to Aβ40 (Roher et al. PNAS).

AmideBio provides the worlds’s highest purity amyloid peptides for research. Using our patented BioPure™ process you can rest assured that your experimental results will not be plagued by uncertainty due to impurities. All AmideBio peptides are >99% pure.

Amyloid β (1-42)

Amyloid β (42-1)

Amyloid β (42-1) SCR

Amyloid β (1-40)

Amyloid β (40-1)