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A1075

Sigma-Aldrich

Amyloid β Protein Fragment 1-40

≥90% (HPLC), powder

Synonym(s):

Aβ40

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About This Item

Empirical Formula (Hill Notation):
C194H295N53O58S
CAS Number:
131438-79-4
Molecular Weight:
4329.80
MDL number:
MFCD00130509
UNSPSC Code:
12352202
NACRES:
NA.32

Quality Level

200

Assay

≥90% (HPLC)

form

powder

color

white

solubility

1% acetic acid: 1 mg/mL
saline: insoluble

UniProt accession no.

P05067

storage temp.

−20°C

Gene Information

human ... APP(351)

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Amino Acid 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

General description

Amyloid β Protein Fragment 1-40 (Aβ40) is derived from the amyloid-β protein (Aβ), which is mapped to human chromosome 21q21.3. Aβ40 is predominantly present in the vascular amyloid deposits. Aβ40 comprises of C-terminal membrane insertion domain. It shows structural transition from random coil to a α-helical structure in a water-micelle medium.

Application

Amyloid β Protein Fragment 1-40 has been used:
  • in the temperature based conformational studies using Fourier transform infrared/differential scanning calorimetry (FT-IR/DSC) studies
  • as a reference standard in sandwich-type enzyme immunoassay for quantifying amyloid A4 protein in cerebrospinal fluid of patients with head trauma
  • as a component of embryonic stem cell medium to inhibit amyloid deposition in fibroblasts

Biochem/physiol Actions

Amyloid β Protein Fragment 1-40 (Aβ40) forms cation based ion channels.
Amyloid β-protein is neurotrophic and neurotoxic in vivo and in vitro in human and rat neuronal cell cultures. β-Amyloid peptides (amino acids 1-42 and 1-43) are the major constituents of senile plaques and neurofibrillary tangles that occur in the hippocampus, neocortex, and amygdala of patients with Alzheimer′s disease.

Reconstitution

For maximal biological activity, dilute the stock in calcium-free PBS to 1 mg/ml and incubate at 37 °C for 4 days.

Other Notes

Lyophilized from 0.1% TFA in H2O

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sigma-Aldrich

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Amyloid β-Protein Fragment 17-40

Yi R Hu et al.
Current Alzheimer research, 18(3), 208-221 (2021-06-10)
Alzheimer's disease (AD) is the most common type of dementia and has a complex pathogenesis with no effective treatment. Energy metabolism disorders, as an early pathological event of AD,have attracted attention as a promising area of AD research. Codonopsis pilosula
D R Howlett et al.
Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration, 4(1), 23-32 (1995-03-01)
The behaviour of synthetic batches of beta-amyloid (beta A) 1-40 peptide in solution has been studied. The effects of beta A1-40 on a PC12 cell toxicity assay was dependent upon the time of preincubation of an aqueous solution of the
M Citron et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(23), 13170-13175 (1996-11-12)
Cerebral deposition of the amyloid beta protein (A beta) is an early and invariant feature of Alzheimer disease (AD). Whereas the 40-amino acid form of A beta (A beta 40) accounts for approximately 90% of all A beta normally released
H Funato et al.
The American journal of pathology, 152(4), 983-992 (1998-04-18)
Amyloid beta-protein (Abeta) is the major component of senile plaques that emerge in the cortex during aging and appear most abundantly in Alzheimer's disease. In the course of our immunocytochemical study on a large number of autopsy cases, we noticed
Solution Structure of Amyloid beta-Peptide (1- 40) in a Water- Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is?
Coles M, et al.
Biochemistry, 37(31), 11064-11077 (1998)
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