β-Amyloid (1-6)-GGC Human DAEFRHGGC-acid
Description
Application Data
Description
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Segment 1-6 of the beta-amyloid 1-42 peptide.
Application Data
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Catalogue number crb1000435 Molecular Weight 990.4 Sequence (one letter code) DAEFRHGGC-acid Sequence (three letter code) H-Asp-Ala-Glu-Phe-Arg-His-Gly-Gly-Cys-OH
Aliase Abeta1-6 Purity >95% Storage -20°C References Lobello et al (2012) Targeting Beta Amyloid: A Clinical Review of Immunotherapeutic Approaches in Alzheimer’s Disease. Int. J. Alzheimers Dis. 628070 PMID: 22292124
Masters and Selkoe (2012) Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease. Cold Spring Harb. Perspect. Med. 2(6) a006262 PMID: 22675658
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 Amino acids 1-6 of amyloid beta peptide (Aβ). This fragment represents an immunogenic portion of Aβ which has been used as the basis for potential immunotherapies for Alzheimer’s disease.
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 a GGC linker, the thiol on the Cysteine can be used for conjugation to dyes and other molecules.