β-Amyloid (10-35), amide

Research use only, not for human use.

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.

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.(In Vitro):β-Amyloid (10-35) is selected based 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)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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Membrane Transporter/Ion Channel

Beta Amyloid

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181427-66-7

2902.33

C133H205N35O36S

>98% (HPLC)

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Sequence: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-NH2

(-20℃)

With Ice Pack

≥ 2 years