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Merck

A1075

Sigma-Aldrich

Amyloid β Protein Fragment 1-40

≥90% (HPLC), powder

Synonym(e):

Aβ40

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About This Item

Empirische Formel (Hill-System):
C194H295N53O58S
CAS-Nummer:
Molekulargewicht:
4329.80
MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.32

Qualitätsniveau

Assay

≥90% (HPLC)

Form

powder

Farbe

white

Löslichkeit

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

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Rekonstituierung

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

Sonstige Hinweise

Lyophilized from 0.1% TFA in H2O

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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)
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
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
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
Diversity of amyloid beta protein fragment [1-40]-formed channels
Kourie JI, et al.
Cellular and Molecular Neurobiology, 21(3), 255-284 (2001)

Artikel

Alzheimer's Disease

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