[TAMRA]-β-Amyloid (1-15) Human


  • Description

  • Application Data


Amino acids 1-15 of amyloid beta protein, a key subunit of extracellular plaques found in the brains of patients with Alzheimer’s disease. Contains N-terminal TAMRA flurophore.

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Application Data

Catalogue number crb1100840
Molecular Weight 2237.9
Sequence (one letter code)


Sequence (three letter code)


Purity >95%
Storage -20°C

Masters and Selkoe, (2012). Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease. Cold Spring Harb. Perspect. Med. 2(6): a006262. PMID: 22675658.

Portelius et al., (2012). Amyloid-β1-15/16 as a Marker for γ-Secretase Inhibition in Alzheimer’s Disease. J. Alzheimer’s Disease. 31(2): 335. PMID: 22531418.

Selkoe and Hardy, (2016). The amyloid hypothesis of Alzheimer’s disease at 25 years. EMBO Mol. Med. 8(6): 595. PMID: 27025652.

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Amyloid beta 1-15 (Aβ1-15) is one of many short Aβ species found in vivo and is formed by the cleavage of amyloid beta precursor protein by β- and α-secretase.

Aβ has been identified as the key subunit of the extracellular plaques found in the brains of patients with Alzheimer’s disease (AD) and Down’s syndrome (DS). Aβ has therefore been extensively studied as a potential target for treatment of AD.

Aβ is formed from the cleavage of the large, transmembrane protein; APP (amyloid precursor protein). Cleavage of APP by β- and then γ-secretases results in the formation of Aβ. Aβ can aggregate to produce amyloid-β oligomers, which are thought to be highly neurotoxic. Over time Aβ can further aggregate to produce the characteristic senile plaques present in AD and DS. Aβ can be degraded by enzymes such as neprilysin, insulin degrading enzyme or endothelin converting enzyme. At physiological levels Aβ may be involved in controlling synaptic activity and neuronal survival.

Contains an N-terminal Carboxytetramethylrhodamine (TAMRA) fluorophore. TAMRA is a pH-stable orange-red fluorescenct dye with good photostability.

[TAMRA]-β-Amyloid (1-15) Human

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When will there be a cure for Alzheimer's Disease? An interview with Dr John Viles

Artilce by Dr Stephen Hoare. I met John Viles in December 2017 to discuss his work on protein misfolding and degenerative diseases. John is a structural biologist in the School of Biological and Chemical Sciences, Queen Mary University of London. He is interested in protein misfolding diseases, of which the main one is Alzheimer’s disease.…

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