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Amyloid-Beta 1-40 Wild type (1.0 mg) Human, Recombinant

Amyloid-Beta 1-40 Wild type (1.0 mg) Human, Recombinant

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    Description

    Article no.: AB-100-10

    Description

    Recombinant Amyloid-Beta-peptide 1-40

    Amount

    1 mg

    Format

    Lyophilized

    Molecular Weight

    4330 Da

    Sequence

    DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

    Purity

    95% by Chromatography and SDS-PAGE

    QC Data



    SDS-PAGE (Coomassie)
    - Single band at ~4 kDa
    - >95% purity

    Mass Spectrometry
    - Observed mass: 4327.1373 Da
    - Theoretical mass: 4329.86 Da

    Note: The images and data shown represent a typical QC batch and may not correspond to the current lot.

    Counter Ion

    Ammonium Acetate

    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.

    Source

    Protein expressed in Escherichia coli.

    Product Citations



















    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 

    Horowitz, S., Koepnick, B., Martin, R., Tymieniecki, A., Winburn, A. A., Cooper, S., … Bardwell, J. C. (2016). Determining crystal structures through crowdsourcing and coursework. Nature communications, 7, 12549. doi:10.1038/ncomms12549

    Luo, J., Wärmländer, S. K., Gräslund, A., & Abrahams, J. P. (2014). Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid β peptide. The Journal of biological chemistry, 289(40), 27766–27775. doi:10.1074/jbc.M114.574947

    Lu, J.-X., Qiang, W., Yau, W.-M., Schwieters, C. D., Meredith, S. C., & Tycko, R. (2013). Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue. Cell, 154(6), 1257–1268. https://doi.org/10.1016/j.cell.2013.08.035

    Schultz, N., Brännström, K., Byman, E., Moussaud, S., Nielsen, H. M., … Olofsson, A. (2018). Amyloid-beta 1-40 is associated with alterations in NG2+ pericyte population ex vivo and in vitro. Aging Cell, 17(3), e12728. https://doi.org/10.1111/acel.12728