Amyloid β-Peptide (12-28) (human) - CAS 107761-42-2
Catalog number: 107761-42-2
Category: Inhibitor
Not Intended for Therapeutic Use. For research use only.
Molecular Formula:
Molecular Weight:
Amyloid β-Peptide (12-28) (human), an Amyloid β-peptide fragment, binds with high affinity to α7-nicotinic ACh receptors. in vivo: Impairs memory retention following central administration in mice.
Brife Description:
Amyloid β-peptide fragment
White lyophilised solid
H-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-OH; Abeta(1-42); Abeta42 protein; amyloid beta-protein (1-42); amyloid-beta-42 peptide; beta-amyloid (1-42); FT-0688953; 107761-42-2
Soluble to 0.70 mg/ml in water
Desiccate at -20°C
Implicated in Alzheimer's disease
Canonical SMILES:
1.Comparison of the amyloid pore forming properties of rat and human Alzheimer's beta-amyloid peptide 1-42: Calcium imaging data.
Di Scala C1, Yahi N1, Flores A1, Boutemeur S1, Kourdougli N2, Chahinian H1, Fantini J1. Data Brief. 2016 Jan 16;6:640-3. doi: 10.1016/j.dib.2016.01.019. eCollection 2016.
The data here consists of calcium imaging of human neuroblastoma SH-SY5Y cells treated with the calcium-sensitive dye Fluo-4AM and then incubated with nanomolar concentrations of either human or rat Alzheimer's β-amyloid peptide Aβ1-42. These data are both of a qualitative (fluorescence micrographs) and semi-quantitative nature (estimation of intracellular calcium concentrations of cells probed by Aβ1-42 peptides vs. control untreated cells). Since rat Aβ1-42 differs from its human counterpart at only three amino acid positions, this comparative study is a good assessment of the specificity of the amyloid pore forming assay. The interpretation of this dataset is presented in the accompanying study "Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides" [1].
2.Overexpression of Swedish mutant APP in aged astrocytes attenuates excitatory synaptic transmission.
Katsurabayashi S1, Kawano H2, Ii M2, Nakano S2, Tatsumi C2, Kubota K3, Takasaki K2, Mishima K3, Fujiwara M2, Iwasaki K3. Physiol Rep. 2016 Jan;4(1). pii: e12665. doi: 10.14814/phy2.12665.
Amyloid precursor protein (APP), a type I transmembrane protein, has different aspects, namely, performs essential physiological functions and produces β-amyloid peptide (Aβ). Overexpression of neuronal APP is responsible for synaptic dysfunction. In the central nervous system, astrocytes - a major glial cell type - have an important role in the regulation of synaptic transmission. Although APP is expressed in astrocytes, it remains unclear whether astrocytic overexpression of mutant APP affects synaptic transmission. In this study, the effect of astrocytic overexpression of a mutant APP on the excitatory synaptic transmission was investigated using coculture system of the transgenic (Tg) cortical astrocytes that express the human APP695 polypeptide with the double mutation K670N + M671L found in a large Swedish family with early onset Alzheimer's disease, and wild-type hippocampal neuron. Significant secretion of Aβ 1-40 and 1-42 was observed in cultured cortical astrocytes from the Tg2576 transgenic mouse that genetically overexpresses Swedish mutant APP.
3.Nanoliposomes protect against human arteriole endothelial dysfunction induced by β-amyloid peptide.
Truran S1, Weissig V2, Madine J3, Davies HA3, Guzman-Villanueva D2, Franco DA1, Karamanova N1, Burciu C1, Serrano G4, Beach TG4, Migrino RQ5. J Cereb Blood Flow Metab. 2016 Feb;36(2):405-12. doi: 10.1177/0271678X15610134. Epub 2015 Oct 8.
We tested whether nanoliposomes containing phosphatidylcholine, cholesterol and phosphatidic acid (NLPA) prevent β-amyloid 1-42 (Aβ42) fibrillation and Aβ42-induced human arteriole endothelial dysfunction. NLPA abolished Aβ42 fibril formation (thioflavin-T fluorescence/electron microscopy). In ex-vivo human adipose and leptomeningeal arterioles, Aβ42 impaired dilator response to acetylcholine that was reversed by NLPA; this protection was abolished by L-NG-nitroarginine methyl ester. Aβ42 reduced human umbilical vein endothelial cell NO production that was restored by NLPA. Nanoliposomes prevented Aβ42 amyloid formation, reversed Aβ42-induced human microvascular endothelial dysfunction and may be useful in Alzheimer's disease.
4.Effects of asiaticoside on human umbilical vein endothelial cell apoptosis induced by Aβ1-42.
Zhang Z1, Cai P2, Zhou J3, Liu M1, Jiang X4. Int J Clin Exp Med. 2015 Sep 15;8(9):15828-33. eCollection 2015.
This study is to investigate the potential role of asiaticoside (AS) in Aβ1-42-induced apoptosis on the human umbilical vein endothelial cell (HUVEC). HUVEC cells were divided into Aβ1-42 group (treated with 50 μM Aβ1-42), AS groups (treated with 50 μM Aβ1-42 and 10 mM, 1 mM, 0.1 mM or 0.01 mM AS), and negative control group (without treatments). Cell proliferation was detected by CCK-8 assay. Apoptosis was analyzed by Hochest33342 staining and flow cytometry. Western Blot was carried out to detect the expression of Bcl-2 and Bax protein. Aβ1-42 treatment inhibited cell proliferation and increased cell apoptosis of HUVEC cells. Interestingly, AS at concentrations of 10 mM, 1 mM, 0.1 mM and 0.01 mM reversed the effects of Aβ1-42 by increasing cell survival rate and reducing apoptosis of HUVEC cells. Furthermore, the expression of Bcl-2 protein was increased whereas the expression of Bax protein was decreased in AS groups. Compared with Aβ1-42 group, the ratio of Bcl-2/Bax was significantly increased in AS groups (P < 0.
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CAS 107761-42-2 Amyloid β-Peptide (12-28) (human)

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