1. Neuronal Signaling
  2. Amyloid-β
  3. β-Amyloid (25-35), HFIP-treated

β-Amyloid (25-35), HFIP-treated  (Synonyms: Amyloid beta-peptide (25-35), HFIP-treated; Aβ25-35, HFIP-treated; β-Amyloid peptide (25-35), HFIP-treated)

Cat. No.: HY-P0128A
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β-Amyloid (25-35) (Amyloid beta-peptide (25-35)), HFIP-treated is a β-Amyloid (25-35) (HY-P0128) treated with HFIP. β-Amyloid (25-35) (Amyloid beta-peptide (25-35)) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide, has shown neurotoxic activities in cultured cells.

For research use only. We do not sell to patients.

β-Amyloid (25-35), HFIP-treated Chemical Structure

β-Amyloid (25-35), HFIP-treated Chemical Structure

CAS No. : 131602-53-4

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Description

β-Amyloid (25-35) (Amyloid beta-peptide (25-35)), HFIP-treated is a β-Amyloid (25-35) (HY-P0128) treated with HFIP. β-Amyloid (25-35) (Amyloid beta-peptide (25-35)) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide, has shown neurotoxic activities in cultured cells[1].

In Vitro

The amino acid sequence of Aβ(25-35) peptide is NH2-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-COOH, where the first Gly represents the amino acid 25 and the last Met represents the amino acid 35. Amyloid beta-peptide(25-35) is also investigated in gel state for the first time. Comparative studies are also carried out using vibrational absorption and ECD. The conformational preference of Aβ(25-35) peptide film is also investigated using vibrational absorption and VCD spectroscopy[1].
Amyloid beta-peptide(25-35) induces apoptotic effects on isolated brain mitochondria and the redox state of methionine-35, plays a key role in the induction of programmed cellular death pathways and toxic events[2].
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. The resulting film is dissolved in anhydrous DMSO at 5 mM and then dilutes into the appropriate concentration and buffer (serum- and phenol red-free culture medium) with vortexing.
2. Next, the solution is age 48 h at 4-8 °C. The sample is then centrifuged at 14000g for 10 min at 4-8 °C; the soluble oligomers are in the supernatant. The supernatant is diluted 10-200-fold for experiments.
Methods vary depends on the downstream applications.

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

Molecular Weight

1060.27

Formula

C45H81N13O14S

CAS No.
Sequence

Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met

Sequence Shortening

GSNKGAIIGLM

SMILES

CSCC[C@@H](C(O)=O)NC([C@H](CC(C)C)NC(CNC([C@H]([C@@H](C)CC)NC([C@H]([C@@H](C)CC)NC([C@H](C)NC(CNC([C@H](CCCCN)NC([C@H](CC(N)=O)NC([C@H](CO)NC(CN)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O

Shipping

Room temperature in continental US; may vary elsewhere.

Storage

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

Purity & Documentation
References
Cell Assay
[2]

Cell viability is determined by a modified MTS assay, which is based on the conversion of Tetrazolium salt by mitochondrial dehydrogenase to a formazan product spectrophotometrically measurable at 490 nm. PC12 cells are plated in 96-well plates at a density of 10 000 cells/well and maintained for 16 h in complete medium. Cells are then incubated in the absence (control) and presence of 40 μM Aβ(31-35) and Aβ(25-35) with reduced, oxidized and norleucine-substituted methionine-35 staurosporine 10 μM is used as positive control of 100% of cellular death. After 48 h of peptide-incubation, 20 μL of MTS reagent (2.0 mg/mL) is added to each well. The cells are then incubated for 30-45 min at 37 °C in a 5% CO2 incubator. The reaction is stopped by adding 25 μL of 10% SDS. The plates are read with a microplate reader at 490 nm. Each data point is obtained using a triplet-well assay[2].

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

References
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β-Amyloid (25-35), HFIP-treated Related Classifications

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β-Amyloid (25-35), HFIP-treated
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