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Amyloid-Beta 1-40 (1.0 mg) Human, Synthetic

Amyloid-Beta 1-40 (1.0 mg) Human, Synthetic

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    Description

    Article no.: AB-150-10

    Description

    Synthetic Amyloid-Beta-peptide 1-40

    Amount

    1mg

    Format

    Lyophilized

    Molecular Weight

    4330 Da

    Sequence

    DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

    Purity

    95% HPLC and SDS-PAGE

    Counter Ion

    TFA (Trifluoracetic Acid)

    Solubility





    Alexotech has developed a proprietary method for preparing the amyloid β-peptide with superior solubility. It is, however, crucial to follow our recommended solubilization procedure. To effectively dissolve the amyloid β-peptide, the pH should be briefly raised to between 11 and 12. This can be achieved by adding 20 mM NaOH. At higher peptide concentrations, a greater NaOH concentration may be required due to the peptide’s intrinsic buffering capacity. The pH should therefore always be monitored and adjusted as necessary. After solubilization, the pH can be brought to the desired level using the buffer of choice.

    Storage

    Store at -20°C upon arrival.

    Product Citations














    Olofsson, A., Lindhagen-Persson, M., Vestling, M., Sauer-Eriksson, A. E., & Öhman, A. (2009). Quenched hydrogen/deuterium exchange NMR characterization of amyloid-β peptide aggregates formed in the presence of Cu2+or Zn2+. FEBS Journal, 276(15), 4051–4060. https://doi.org/10.1111/j.1742-4658.2009.07113.x

    Lindhagen-Persson, M., Brännström, K., Vestling, M., Steinitz, M., & Olofsson, A. (2010). Amyloid-β Oligomer Specificity Mediated by the IgM Isotype – Implications for a Specific Protective Mechanism Exerted by Endogenous Auto-Antibodies. PLoS ONE, 5(11), e13928. https://doi.org/10.1371/journal.pone.0013928

    Brunetti, D., Torsvik, J., Dallabona, C., Teixeira, P., Sztromwasser, P., Fernandez-Vizarra, E., … Bindoff, L. A. (2015). Defective PITRM1 mitochondrial peptidase is associated with A  amyloidotic neurodegeneration. EMBO Molecular Medicine, 8(3), 176–190. https://doi.org/10.15252/emmm.201505894

    Lindberg, D. J., Wranne, M. S., Gilbert Gatty, M., Westerlund, F., & Esbjörner, E. K. (2015). Steady-state and time-resolved Thioflavin-T fluorescence can report on morphological differences in amyloid fibrils formed by Aβ(1-40) and Aβ(1-42). Biochemical and Biophysical Research Communications, 458(2), 418–423. https://doi.org/10.1016/j.bbrc.2015.01.132