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| Home > Publications database > Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide |
| Journal Article | PreJuSER-60107 |
; ; ;
2007
Science Direct
New York, NY [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.jchromb.2007.06.003
Abstract: The amyloid cascade hypothesis assigns the amyloid-beta peptide (Abeta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of Abeta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant Abeta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify Abeta(1-42), which is fully cytotoxic and able to form fibrils without any further refolding steps. The yield of the procedure is 5-8 mg of tag-less peptide per liter culture volume.
Keyword(s): Amino Acid Sequence (MeSH) ; Amyloid beta-Peptides: isolation & purification (MeSH) ; Amyloid beta-Peptides: pharmacology (MeSH) ; Base Sequence (MeSH) ; Chromatography, High Pressure Liquid (MeSH) ; DNA Primers (MeSH) ; Humans (MeSH) ; Molecular Sequence Data (MeSH) ; Peptide Fragments: isolation & purification (MeSH) ; Peptide Fragments: pharmacology (MeSH) ; Recombinant Proteins: isolation & purification (MeSH) ; Recombinant Proteins: pharmacology (MeSH) ; Amyloid beta-Peptides ; DNA Primers ; Peptide Fragments ; Recombinant Proteins ; amyloid beta-protein (1-42) ; J ; purification (auto) ; amyloid-beta peptide (auto) ; cytotoxicity (auto) ; aggregation (auto) ; Alzheimer's disease (auto)
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