β-Amyloid (1-42), human TFA

For research use only. Not for therapeutic Use.

  • CAT Number: I046308
  • Molecular Formula: C205H312F3N55O62S
  • Molecular Weight: 4628.06
  • Purity: ≥95%
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β-Amyloid (1-42), human TFA (Amyloid β-Peptide (1-42) (human) TFA) is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease[1][2][3].
β-Amyloid Aggregation Guidelines (Following is our recommended protocol. This protocol only provides a guideline, and should be modified according to your specific needs).
1. Solid Aβ peptide was dissolved in cold hexafluoro-2-propanol (HFIP). The peptide was incubated at room temperature for at least 1h to establish monomerization and randomization of structure.
2. The HFIP was removed by evaporation, and the resulting peptide was stored as a film at -20 or -80°C.
3. The resulting film was dissolved in anhydrous DMSO at 5 mM and then diluted into the appropriate concentration and buffer (serum- and phenol-red-free culture medium) with vortexing.
4. Next, the solution was age 48h at 4-8°C. The sample was then centrifuged at 14000g for 10 min at 4-8°C; the soluble oligomers were in the supernatant. The supernatant was diluted 10-200-fold for experiments.
Methods vary depends on the downstream applications.
Note:
The aggregation form is unstable in the solution, it is recommended to use it immediately.
β-Amyloid (1-42), human TFA can be used in animal modeling to construct Alzheimer’s disease models.


Catalog Number I046308
Molecular Formula C205H312F3N55O62S
Purity ≥95%
Reference

[1]. Solntseva EI, et al. Impact of amyloid-β peptide (1-42) on voltage-gated ion currents in molluscan neurons. Bull Exp Biol Med. 2011 Oct;151(6):671-4.
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[2]. Barucker C, et al. Nuclear translocation uncovers the amyloid peptide Aβ42 as a regulator of gene transcription. J Biol Chem. 2014 Jul 18;289(29):20182-91.
 [Content Brief]

[3]. Stefania Sabella, et al. Capillary electrophoresis studies on the aggregation process of beta-amyloid 1-42 and 1-40 peptides. Electrophoresis. 2004 Oct;25(18-19):3186-94.
 [Content Brief]

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