β-Amyloid (1-42), human, HFIP-treated 

β-Amyloid (1-42), human, HFIP-treated is a β-Amyloid (1-42), human (HY-P1363A) treated with HFIP. β-Amyloid (1-42), human (Amyloid β-Peptide (1-42) (human)) is a 42-amino acid peptide that causes neurotoxicity, which is related to the pathogenesis of Alzheimer's disease. β-Amyloid (1-42), human specifically interacts with the promoters of genes like LRP1 and KAI1. β-Amyloid (1-42), human can form oligomers and fibrils in vitro, and the oligomeric form is more neurotoxic than the fibrillar form^{[1][2][3][4][5][6]}.

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. β-Amyloid (1-42), human, HFIP-treated is 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.
2. Next, the solution is age 48h at 4-8°C. The sample is then centrifuged at 14000g for 10 min at 4-8°C; the soluble oligomers were in the supernatant. The supernatant is 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.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

4514.04

C₂₀₃H₃₁₁N₅₅O₆₀S

107761-42-2

Viscous Liquid

Colorless to light yellow

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Shipping with dry ice.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [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.  [Content Brief]

  [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]

  [4]. Vosough F, et al. Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size. ACS Chem Neurosci. 2021 Feb 3;12(3):473-488.  [Content Brief]

  [5]. Stine WB Jr, et al. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem. 2003 Mar 28;278(13):11612-22.  [Content Brief]

  [6]. Roher AE, et al. beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10836-40.  [Content Brief]