PP69

β-Amyloid Peptide (1-42), Human

• Synonym(s): β-Amyloid Peptide (1-42), Human, DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
• Empirical Formula (Hill Notation): C₂₀₃H₃₁₂N₅₆O₅₉S
• Molecular Weight: 4513.05
• NACRES: NA.77
• UNSPSC Code: 12352202

Properties

• assay: ≥95% (HPLC)
• Quality Segment: 100
• form: lyophilized
• does not contain: preservative
• manufacturer/tradename: Calbiochem^®
• storage condition: OK to freeze, desiccated (hygroscopic)
• dilution: (Substrate Cleavage Assays (30-100 μg/mL))
• solubility: 50 mM Tris-HCl, pH >9.0: ≤1 mg/mL
• shipped in: ambient
• storage temp.: −20°C

Description

General description

Wild-type, human Aβ_1-42 peptide. A number of mutations, identified in the gene encoding the β-amyloid precursor protein (βAPP), have been linked to early-onset Familial Alzheimer’s Disease. Mutations in the genes encoding presenilin 1 and presenilin 2 have also been shown to alter the processing of βAPP, resulting in increased extracellular concentration of β-amyloid peptide Aβ1-42(43) relative to Aβ1-40. Biophysical and biochemical experiments suggest that Aβ1-42(43) may serve as a catalyst for the aggregation and deposition of β-amyloid peptide (Aβ) leading to neurotoxic effects associated with senile plaque formation. Furthermore, antibodies recog-nizing Aβ1-42 revealed that the long form of the peptide is increased in presenilin and βAPP mutants, while other studies have used Aβ specific antibodies to prevent the in vitro fibrillar aggregation of Aβ. Amino acid sequence verified by amino acid analysis or sequencing. This product is supplied in a form that is not neurotoxic prior to a preincubation step. The appearance of toxicity has recently been shown to correlate to the extent of β sheet structure. Useful for neurotoxicity studies and substrate cleavage assays.

Immunogen

Human

Application

Substrate Cleavage Assays (30-100 μg/ml)

Physical form

Supplied as a chloride salt.

Preparation Note

Reconstitute just prior to use. Do not store following reconstitution, as aggregation may occur.

Other Notes

Citron, M., et al. 1997. Nature Med.3, 67.
Hardy, J. 1997. Trends in Neurosci.20, 154.
Solomon, B., et al. 1997. Proc. Natl. Acad. Sci. USA94, 4109.
Duff, K., et al. 1996. Nature 383, 710.
Iwatsubo, T., et al. 1994. Neuron13, 45.
Suzuki, N., et al. 1994. Science264, 133.
Simmons, L.K., et al. 1994. Mol. Pharmacol.45, 373.

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

Synthetic peptide corresponding to amino acid residues 1 - 42 of the processed human β-amyloid peptide.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)

Safety Information

• Storage Class: 11 - Combustible Solids
• wgk: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable