A9810
Amyloid β Protein Fragment 1-42
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About This Item
Formule empirique (notation de Hill):
C203H311N55O60S
Numéro CAS:
Poids moléculaire :
4514.04
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
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
Description générale
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
Actions biochimiques/physiologiques
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
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)
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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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