Amyloid-Beta 1-40, 15N Uniform Label (1.0 mg) Human, Recombinant

Description

Recombinant Amyloid-Beta-Peptide (1-40) uniformly ¹⁵N labeled

Amount

1mg

Format

Lyophilized

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: 4377.0047 Da
- Theoretical mass (Without 15N Uniform Labeling): 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 using ¹⁵NH₄-Cl as sole nitrogen source.

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

Brännström, K., Öhman, A., & Olofsson, A. (2011). Aβ Peptide Fibrillar Architectures Controlled by Conformational Constraints of the Monomer. PLoS ONE, 6(9), e25157. https://doi.org/10.1371/journal.pone.0025157

Lindgren, J., Wahlström, A., Danielsson, J., Markova, N., Ekblad, C., Gräslund, A., … Wärmländer, S. K. (2010). N-terminal engineering of amyloid-β-binding Affibody molecules yields improved chemical synthesis and higher binding affinity. Protein science : a publication of the Protein Society, 19(12), 2319–2329. doi:10.1002/pro.511

Wallin, C., Kulkarni, Y. S., Abelein, A., Jarvet, J., Liao, Q., Strodel, B., … Wärmländer, S. K. T. S. (2016). Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer⿿s disease. Journal of Trace Elements in Medicine and Biology, 38, 183–193. https://doi.org/10.1016/j.jtemb.2016.03.009

Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2014). Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid β Peptide. Journal of Biological Chemistry, 289(40), 27766–27775. https://doi.org/10.1074/jbc.m114.574947