2. Neuronal Signaling
  3. Amyloid-β
  4. β-Amyloid (1-40), HFIP-treated

β-Amyloid (1-40), HFIP-treated is a β-Amyloid (1-40) (HY-P0265A) treated with HFIP. β-Amyloid (1-40) is a primary protein in plaques found in the brains of patients with Alzheimer's disease.

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β-Amyloid (1-40), HFIP-treated

β-Amyloid (1-40), HFIP-treated Chemical Structure

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β-Amyloid (1-40), HFIP-treated Related Antibodies

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Description

β-Amyloid (1-40), HFIP-treated is a β-Amyloid (1-40) (HY-P0265A) treated with HFIP. β-Amyloid (1-40) is a primary protein in plaques found in the brains of patients with Alzheimer's disease[1].

In Vivo

Note:
Please do not refer to only one article to determine the experimental conditions. It is recommended to determine the optimal experimental conditions (animal strain, age, dosage, frequency and cycle, detection time and indicators, etc.) through preliminary experiments before the formal experiment.

β-Amyloid (1-40) can be used in animal modeling to create Alzheimer's disease models.

Induction of Alzheimer's disease[2]
Background
β-Amyloid (1-40) induces Alzheimer's disease by accumulating in the brain and being neurotoxic.
Specific Modeling Methods
Rat: Wistar • male • 280-320 g
Administration: 0, 3, 30, 300 pmol • connection of cannulae to modified micro-osmotic pumps for infusion • 2 weeks
Note
(1) Dissolve β-Amyloid (1-40) in 35% acetonitrile/0.1% trifluoroacetic acid (TFA).
(2) In each group of 7 rats, a catheter was placed into the left ventricle on day 1. A water maze task was performed on days 9-13 after the start of infusion. At the end of the behavioural experiments, 4 rats from each group were taken from each group and processed by severing their heads for ChAT activity assay. Three rats were taken for histochemical studies.
(3) In histochemical studies, rats were anaesthetised and executed by transaortic perfusion fixation, first in cold saline and then in 4% paraformaldehyde and 0.1 M sodium phosphate buffer. Brains were removed and fixed in the same fixative for 12 hours. Frozen brain tissue was cut at 20 μm using a cryostat and the periventricular region was collected.
Modeling Indicators
Molecular changes: The activity of acetyltransferase (ChAT) in the frontal cortex and hippocampus is reduced, and cholinergic neuron dysfunction occurs.
Organizational changes: Accumulation of β-Amyloid in the hippocampus and cerebral cortex.
Phenotypic observation: Memory impairment occurs.
Correlated Product(s): /
Opposite Product(s): /

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

4329.80

Formula

C194H295N53O58S
Sequence

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
Sequence Shortening

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV
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
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β-Amyloid (1-40), HFIP-treated Related Classifications

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Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

Keywords:

β-Amyloid (1-40), HFIP-treatedAmyloid-ββ-amyloid peptideAβAbetaInhibitorinhibitorinhibit

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