Amyloid Beta Peptide (1-42)(A42-58)
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Description :The Amyloid Beta Peptide (42 aa) sequence is DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA. It is produced synthetically and treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) prior to drying which breaks down pre-formed fibrils and monomerizes the peptide.
Sequence :DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Genbank Number :P05067
Alternative Names :Abeta Protein; Abeta peptide; Amyloid beta precursor protein peptide; APP
Purity :Certified >95% pure using mass spec and HPLC.
Formulation :Peptide supplied as a dried peptide film.
Storage and Stability :Store product at –20oC. For optimal storage, aliquot diluted product into smaller quantities and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Reconstitution Protocol :It is recommended the re-suspended peptide is kept on ice and used immediately to avoid aggregation. While several methods of monomer resuspension are detailed in the literature, we recommend the following protocol for resuspending 1 mg of peptide into a 1mg/mL solution.
1. Bring dried peptide to room temperature for 10 minutes.
2. Freshly open a sealed vial of DMSO (Sigma Hybri-Max D2650). Fresh DMSO is critical as it will absorb water over time, which can affect re-suspension as soluble monomer.
3. Add 20 µL fresh DMSO to peptide aliquot, mix well by pipetting up and down. Take care to scrape inside lower walls of tube to ensure complete resuspension of the film. Do not store DMSO stock on ice as it will freeze.
4. Vortex DMSO stock for 10 seconds, bath sonicate for 10 minutes.
5. Add 980 µL of cold filter sterilized dH2O. Optional – Centrifuge monomer 14,000 x g for 5 minutes at 4°C and keep supernatant to remove any material that was not fully resuspended.
6. Keep monomer on ice and use immediately.
Sample Data :Western blot of amyloid 1-42 monomers (left), oligomers (middle), and fibrils (right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed until TEM/AFM show a signal greater than 100 kDa and a distinct signal in the stacking gel (right). 
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