β-Amyloid (12-28) (Amyloid β-Protein (12-28)) is a peptide fragment of β-amyloid protein (β1-42). β1-42, a 42 amino acid protein , is the major component of senile plaque cores. β-Amyloid (12-28) shows aggregation properties. β-Amyloid (12-28) has the potential for Alzheimer’s disease research^[1].

Amyloid-β^[1]

β-amyloid (12-28) may exert dysregulation cognitive effects by means of defective coordination of potassium channel function in nerve, glia and endothelial cells^[1].
β-Amyloid Aggregation Guidelines (Following is our recommended protocol. This protocol only provides a guideline, and should be modified according to your specific needs).
1. Solid Aβ peptide was dissolved in cold hexafluoro-2-propanol (HFIP). The peptide was incubated at room temperature for at least 1h to establish monomerization and randomization of structure.
2. The HFIP was removed by evaporation, and the resulting peptide was stored as a film at -20 or -80 ℃.
3. The resulting film was dissolved in anhydrous DMSO at 5 mM and then diluted into the appropriate concentration and buffer (serum- and phenol red-free culture medium) with vortexing.
4. Next, the solution was age 48h at 4-8 ℃. The sample was then centrifuged at 14000g for 10 min at 4-8 ℃; the soluble oligomers were in the supernatant. The supernatant was diluted 10-200-fold for experiments.
Methods vary depends on the downstream applications.

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

1955.18

C₈₉H₁₃₅N₂₅O₂₅

107015-83-8

Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys

VHHQKLVFFAEDVGSNK

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Rabanal F, et al. Structural, kinetic and cytotoxicity aspects of 12-28 beta-amyloid protein fragment: a reappraisal. J Pept Sci. 2002 Oct;8(10):578-88.

  [2]. Nikunj S Patel, et al. Potent anti-angiogenic motifs within the Alzheimer beta-amyloid peptide. Amyloid. 2008 Mar;15(1):5-19.

PC12 pheochromocytoma cell lines are routinely cultured in Dulbecco’s modified Eagle’s medium containing 10% fetal bovine serum,5% horse serum, 1% glutamine and 1% penicillin/streptomycin. Exponentially growing cellsare plated at 30000 cells per well per 100 µL of fresh medium in 96-well tissue cultures plates. Toxicity assays are carried out by measurementof MTT reduction. Two days after plating PC12 pheochromocytoma cell lines are treated with different concentrations of aged β-amyloid (12-28). After 22 h, MTT (5 mg/mL) wasadded and incubation is continued for a further2 h. Cells are lysed and after 24 h at 37°C,colorimetric determination of MTT reduction is made at 550 nm. Positive controls consist of cells in culture medium. Assay values obtained with these controls are taken as 100% viability^[1].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

• [1]. Rabanal F, et al. Structural, kinetic and cytotoxicity aspects of 12-28 beta-amyloid protein fragment: a reappraisal. J Pept Sci. 2002 Oct;8(10):578-88.

  [2]. Nikunj S Patel, et al. Potent anti-angiogenic motifs within the Alzheimer beta-amyloid peptide. Amyloid. 2008 Mar;15(1):5-19.