Pyroglutamyl β-Amyloid (4-14) Biotin is derived from Amyloid-β, which 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).
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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
Pyroglutamyl β-Amyloid (4-14) Biotin is derived from Amyloid-β, which 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.
This peptide contains a C-terminal Biotin tag that is covalently bonded via ethylenediamine and can be used for detection and purification. Addionally, there is a Pyroglutamyl molecule located at the N-terminal position.
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