产品
编 号：F225833
分子式：C133H205N35O36S
分子量：2902.33
分子式：C133H205N35O36S
分子量：2902.33
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CAS No: 181427-66-7
产品详情
生物活性：
β-Amyloid (10-35), amide is composed of 26 aa (10-35 residues of the Aβ peptide) and is the primary component of the amyloid plaques of Alzheimer’s disease.
体外研究：
β-Amyloid (10-35)is selectedbased on the following considerations: (1) β-Amyloid (10-35) incorporates the core region, point mutations of which significantly obstruct fibril formation and have been used to generate inhibitors of fibrillogenesis; (2) β-Amyloid (10-35) retains the ability to add to bona fide Alzheimer’s plaques, in contrast to other truncated peptides, and forms fibrils morphologically similar to those of the full length peptide; (3) Of most importance, the full length peptide, Aβ(1-42), is intractable for the controlled formation of fibrils from aqueous media because at the earliest time points, some of the peptide exists as an amorphous precipitate. In contrast, the use of β-Amyloid (10-35) allows the reproducible and controlled formation of fibrils from aqueous solutions, under defined conditions of pH, ionic strength, and peptide concentration and thus yields the required homogeneous fibrils.
β-Amyloid (10-35), amide is composed of 26 aa (10-35 residues of the Aβ peptide) and is the primary component of the amyloid plaques of Alzheimer’s disease.
体外研究：
β-Amyloid (10-35)is selectedbased on the following considerations: (1) β-Amyloid (10-35) incorporates the core region, point mutations of which significantly obstruct fibril formation and have been used to generate inhibitors of fibrillogenesis; (2) β-Amyloid (10-35) retains the ability to add to bona fide Alzheimer’s plaques, in contrast to other truncated peptides, and forms fibrils morphologically similar to those of the full length peptide; (3) Of most importance, the full length peptide, Aβ(1-42), is intractable for the controlled formation of fibrils from aqueous media because at the earliest time points, some of the peptide exists as an amorphous precipitate. In contrast, the use of β-Amyloid (10-35) allows the reproducible and controlled formation of fibrils from aqueous solutions, under defined conditions of pH, ionic strength, and peptide concentration and thus yields the required homogeneous fibrils.
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