Home>>Peptides>>β-amyloid (12-28) (TFA)

β-amyloid (12-28) (TFA) (Synonyms: Amyloid β-Protein (12-28) (TFA); Amyloid Beta-Peptide (12-28) (human) TFA; β-Amyloid protein fragment(12-28) TFA)

Catalog No.GC61988

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β-amyloid (12-28) (TFA) Chemical Structure

Size Price Stock Qty
1 mg
$108.00
In stock
5 mg
$270.00
In stock

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Sample solution is provided at 25 µL, 10mM.

Description Chemical Properties Product Documents

β-amyloid (12-28) TFA 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].

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.

[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.

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