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

β-Amyloid (1-42), human, HFIP-treated, a 42-amino acid peptide that has been treated with HFIP from β-Amyloid (1-42), human (HY-P1363A), is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human, HFIP-treated remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, HFIP-treated, after being dissolved in DMSO to form the stock solution, on the one hand, can form soluble oligomers (AβOs) when incubated at 4 ℃, which have synaptic toxicity and neurotoxicity; on the other hand, it can be incubated at 37 ℃ to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death^{[1][2][3][4][5][6][7]}.

β-淀粉样蛋白聚集指南（以下是我们推荐的方案。该方案仅提供指南，应根据您下游实验方案的具体需求进行修改）。
寡聚体制备：
1. 将 β-Amyloid (1-42), human, HFIP-treated 溶解于无水 DMSO 中，浓度为 5 mM，然后涡旋稀释至适当浓度和缓冲液 (冰冷的 PBS/无血清无酚红的 DMEM/F12 培养基) 中。
2. 接下来，将溶液在 4-8 °C 下陈化 24-48 小时。然后将样品在 4-8 °C 下以 14000 g 离心 10 分钟；可溶性低聚物在上清液中。将上清液稀释 10-200 倍用于实验。
纤维体制备：
1. 将 β-Amyloid (1-42), human, HFIP-treated 溶解于无水 DMSO中，浓度为 5 mM，然后用涡旋混合稀释到适当的浓度和缓冲液 (10 mM HCl) 中。
2. 接下来，将溶液在 37 °C 下陈化 24-48 小时，得到 Aβ42 纤维体。
注意：
1) 在进行步骤 1 时，如有少量不溶物，可延长 HFIP 处理时间 (如过夜孵育)、涡旋震荡、或辅助短时间超声；如仍有少量不溶物，建议离心或过滤去除。
2) 聚集形式在溶液中不稳定，建议现配现用。如需储存，建议以薄膜形式的肽储存在 -20 或 -80 °C 下。
β-Amyloid (1-42), human, HFIP-treated 制备成寡聚体，具有神经毒性：
β-amyloid (1-42) peptide (60-180 μM, 48 小时) 形成寡聚体的速度明显快于 Aβ40 和 Aβ43，Aβ42 寡聚体 (1-1000 μg/mL, 48 小时) 在 SH-SY5Y 和 PC12 细胞中表现出最高的神经毒性^[10]。
Aβ42 oligomers (20 μM, 0-48 小时) 会促使 SH-SY5Y 细胞发生凋亡和自噬，而 U87 细胞则仅发生自噬^[11]。
Aβ42 oligomers (0.5 μM, 1 小时) 会导致小鼠神经母细胞瘤 N2a 细胞内钙离子内流、线粒体活性氧 (ROS) 生成，并增加细胞死亡率^[12]。

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

4514.04

C₂₀₃H₃₁₁N₅₅O₆₀S

107761-42-2

粘稠液体

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]. Porzoor A, et al. Pretreatment of chemically-synthesized Aβ42 affects its biological activity in yeast. Prion. 2014;8(6):404-10.  [Content Brief]

  [5]. Zou K, et al. A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. J Neurosci. 2002 Jun 15;22(12):4833-41.  [Content Brief]

  [6]. Peters C, et al. Alzheimer's Aβ interacts with cellular prion protein inducing neuronal membrane damage and synaptotoxicity. Neurobiol Aging. 2015 Mar;36(3):1369-77.  [Content Brief]

  [7]. Yao ZX, et al. Function of beta-amyloid in cholesterol transport: a lead to neurotoxicity. FASEB J. 2002 Oct;16(12):1677-9.  [Content Brief]

  [8]. Jancsó G, et al. Beta-amyloid (1-42) peptide impairs blood-brain barrier function after intracarotid infusion in rats. Neurosci Lett. 1998 Sep 4;253(2):139-41.  [Content Brief]

  [9]. Bourgade K, et al. β-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1. Biogerontology. 2015 Feb;16(1):85-98.  [Content Brief]

  [10]. Fu L, et al. Comparison of neurotoxicity of different aggregated forms of Aβ40, Aβ42 and Aβ43 in cell cultures. J Pept Sci. 2017 Mar;23(3):245-251.  [Content Brief]

  [11]. Wang H, et al. Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells. J Alzheimers Dis. 2010;21(2):597-610.  [Content Brief]

  [12]. Fei X, et al. Degradation of FA reduces Aβ neurotoxicity and Alzheimer-related phenotypes. Mol Psychiatry. 2021 Oct;26(10):5578-5591.  [Content Brief]