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A9810

Sigma-Aldrich

Amyloid β Protein Fragment 1-42

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About This Item

Empirical Formula (Hill Notation):
C203H311N55O60S
CAS Number:
Molecular Weight:
4514.04
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

Assay

≥95% (HPLC)

Quality Level

form

powder

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... APP(351)

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-Ile-Ala

General description

Amyloid β Protein is produced from amyloid-β precursor protein (APP). It consists of two C terminal variants, such as a long tailed Aβ 1-42 and a short tailed Aβ 1-40. APP is located on human chromosome 21q21.3.

Application

Amyloid β Protein Fragment 1-42 has been used:
  • for the preparation of Aβ 1-42 oligomer
  • for western blot analysis
  • for the interference test of immunomagnetic reduction (IMR) plasma Aβ42 assay
  • to study the effects of resveratrol on Aβ 1-42-induced impairment of spatial learning, memory and synaptic plasticity
  • to investigate the effect of Aβ in epithelial cell culture

Biochem/physiol Actions

Amyloid β Protein Fragment 1-42 (Aβ 1-42) has antioxidant and neuroprotective properties. Accumulation of amyloid β Protein is associated with Alzheimer′s disease (AD) and Down Syndrome. Aβ 1-42 regulates cholesterol transport and may function as a transcription factor. It may possess anti-inflammatory and antimicrobial properties.
The predominant fragment of amyloid β-protein found in the brains of patients with Alzheimer′s disease and Down′s syndrome.

related product

Product No.
Description
Pricing

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Resveratrol ameliorates spatial learning memory impairment induced by Abeta1-42 in rats
Wang R, et al.
Neuroscience, 344, 39-47 (2017)
Alzheimer's disease and the amyloid-beta peptide
Murphy MP and LeVine III H
Journal of Alzheimer'S Disease, 19(1), 311-323 (2010)
Molecular genetics of Alzheimer disease amyloid.
Tanzi RE, et al
The Journal of biological chemistry, 266(31), 20579-20582 (1991)
Jeremy D Baker et al.
PLoS biology, 15(6), e2001336-e2001336 (2017-06-28)
The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in tauopathies, the most common of which
Kyunghee Byun et al.
PloS one, 7(5), e37917-e37917 (2012-06-05)
Advanced glycation end products (AGEs) have long been considered as potent molecules promoting neuronal cell death and contributing to neurodegenerative disorders such as Alzheimer's disease (AD). In this study, we demonstrate that AGE-albumin, the most abundant AGE product in human

Articles

Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions.

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