Amyloid-Beta 1-40, 15N Uniform Label (0.2 mg) Human, Recombinant

Description

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

Amount

0.2mg

Format

Lyophilized

Sequence

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

Purity

95% by Chromatography and SDS-PAGE

Counter Ion

Ammonium Acetate

Solubility

Alexotech has developed a proprietary technique of preparing the amyloid β-peptide (1-40) having a superior solubility. It is however, of utmost importance to follow our recommendations of solubilisation: To efficiently solubilise the amyloid β-peptide (1-40) the pH should briefly be raised to between 11-12. This can be accomplished by 20 mM of NaOH, however, at high peptide concentrations a higher NaOH concentration may be required due to the intrinsic buffering capacity of the peptide. The pH should therefore always be monitored and if necessary adjusted. After solubilisation the pH can be adjusted 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