Labeled Amyloid Peptides
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Labeled Amyloid Peptides

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Cat. # Product Name Price
A13223Beta-Amyloid (1-28), FAM--labeledInquiry
CAD-011Biotinyl-Amyloid β-Protein (1-40)Inquiry
CAD-012Biotinyl-εAhx-Amyloid β-Protein (1-40)Inquiry
CAD-013(7-Diethylaminocoumarin-3-yl)carbonyl-Amyloid β-Protein (1-40)Inquiry
CAD-0145-FAM-Amyloid β-Protein (1-40)Inquiry
CAD-015FITC-β-Ala-Amyloid β-Protein (1-40)Inquiry
CAD-0165-TAMRA-Amyloid β-Protein (1-40)Inquiry
CAD-017Biotinyl-Amyloid β-Protein (1-42)Inquiry
CAD-018Biotinyl-εAhx-Amyloid β-Protein (1-42)Inquiry
CAD-0195-FAM-Amyloid β-Protein (1-42)Inquiry
CAD-020FITC-β-Ala-Amyloid β-Protein (1-42)Inquiry
CAD-021FITC-εAhx-Amyloid β-Protein (1-42)Inquiry
CAD-0225-TAMRA-Amyloid β-Protein (1-42)Inquiry


APP (Amyloid protein precursor) amyloid precursor protein is a large cell membrane protein whose N-terminus extends out of the cell. The protein is destroyed and a 42 amino acid beta-amyloid peptide is released, which is found in senile plaques and blood vessels. These abnormal proteins may accumulate, leading to cellular disorders and neuronal damage. Those labeled amyloid peptides is important in studying the relationship between APP and Alzheimer’s Disease (AD). For example, the biotinylated amyloid beta (1-40) antibody is a multifunctional cytokine that can be produced by both lymphocytes and non-lymphocytes. It plays an important role in the regulation of immune response, blood cell proliferation, defense mechanism and acute phase response. IL6 is a glycoprotein that induces the production of related proteins in the acute phase. It is also an essential factor for the differentiation and secretion of antibodies in beta cells. It plays an important role in immune regulation. The precursor of human IL-6 has 212 Amino acids. The mature form is 185 amino acids.

Mechanism of action

Electron paramagnetic resonance spectroscopy of 19 spin-labeled derivatives of Alzheimer’s disease amyloid beta (Aβ) peptide was used to reveal structural features of amyloid fibril formation. In fibrils, a wide range of peptides show aligned parallel alignments. Based on parallel alignment and side chain mobility analysis, scientists found that most of the amyloid structure is ordered and specific, but they also identified more dynamic regions (N and C ends) and may turn or bend regions (residual Base 23-26). Although they have different aggregation characteristics and effects in the disease, the two peptides Aβ40 and Aβ42 are uniformly blended in the amyloid fibrils, indicating that they have the same structure.

Application of Labeled amyloid peptides

A significant pathological feature of Alzheimer’s disease (AD) is the presence of high density amyloid plaques in the victim’s brain tissue. Plaques are mainly composed of human β-amyloid peptide (βA4), which is a 40-mer whose neurotoxicity is associated with its aggregation. Radioactive iodine-labeled human β4A was rapidly deposited from dilute (less than 10 pM) solution into neuritis and diffuse plaques and cerebrovascular amyloid in AD brain tissue in vitro, whereas no deposition is detectable in tissue without performed plaques. Labeled amyloid peptides are thought to play a role in the development of the senile plaques associated with Alzheimer’s Disease.

1. Maggio, J. E., Stimson, E. R., Ghilardi, J. R., Allen, C. J., Dahl, C. E., Whitcomb, D. C., ... & Mantyh, P. W. (1992). Reversible in vitro growth of Alzheimer disease beta-amyloid plaques by deposition of labeled amyloid peptide. Proceedings of the National Academy of Sciences, 89(12), 5462-5466.
2. T?r?k, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., & Langen, R. (2002). Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling. Journal of Biological Chemistry, 277(43), 40810-40815.
3. Murpy, M. P., & LeVine III, H. (2010). Alzheimer’s disease and the β-amyloid peptide. J Alzheimers Dis, 19(1), 311-323.

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