β-amyloïde (1-42), humaan, met HFIP behandeld

β-Amyloid (1-42), human, HFIP-treated, a 42-amino acid peptide that has been treated with HFIP from β-Amyloid (1-42), human , 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°C, which have synaptic toxicity and neurotoxicity; on the other hand, it can be incubated at 37°C 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].

107761-42-2

12352209

Amyloid-β

Neuronal Signaling

Neuroscience-Neurodegeneration

Neurological Disease

99.89

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C203H311N55O60S

4514.04

[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. |[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. |[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. |[4]Porzoor A, et al. Pretreatment of chemically-synthesized Aβ42 affects its biological activity in yeast. Prion. 2014;8 (6) :404-10.|[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.|[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.|[7]Yao ZX, et al. Function of beta-amyloid in cholesterol transport: a lead to neurotoxicity. FASEB J. 2002 Oct;16 (12) :1677-9.|[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.|[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.|[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.|[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.|[12]Fei X, et al. Degradation of FA reduces Aβ neurotoxicity and Alzheimer-related phenotypes. Mol Psychiatry. 2021 Oct;26 (10) :5578-5591.

Dry Ice

-80°C, sealed storage, away from moisture and light

http://file.medchemexpress.com/batch_PDF/HY-P1363B/β-Amyloid-1-42-human-HFIP-treated-SDS-MedChemExpress.pdf

Peptides

No Development Reported