[5-FAM]-β-Amyloid (1-40) Human [5-FAM]-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-acid
Amyloid beta (Aβ) protein 1-40, constituting the most abundant Aβ peptide in the human brain. Contains N-terminal Fluorescein (FAM) molecule
Catalogue number crb1100842 Sequence (one letter code) [5-FAM]-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-acid Sequence (three letter code)
Purity >95% Storage -20°C References
Masters and Selkoe (2012) Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease. Cold Spring Harb. Perspect. Med. 2(6) a006262 PMID: 22675658
Pearson and Peers (2006) Physiological roles for amyloid β peptides. J. Physiol. 575(1) 5 PMID: 16809372
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
Fluorescein (FAM) labelled amyloid beta protein 1-40 (Aβ 1-40). Aβ 1-40 is a major C terminal variant of amyloid beta constituting the most abundant Aβ peptide in the human brain.
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.
Fluorescein is a hugely popular fluorescent tag due to its excellent fluorescence quantum yield and relatively high absorptivity as well as being highly water soluble.