Peptides

Beta-Amyloid (1-42), HiLyte™ Fluor 488-labeled - 0.1 mg

293.00
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  • Cat.Number : AS-60479-01
  • Availability :
    In production

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Aß (1-42), a major component of amyloid plaques, accumulates in neurons of Alzheimer’s disease brains. Biochemical analysis of the amyloid peptides isolated from Alzheimer’s disease brain indicates that Aß (1-42) is the principal species associated with senile plaque amyloids, while Aß (1-40) is more abundant in cerebrovascular amyloid deposit. This is a fluorescent (HiLyte™ Fluor 488)-labeled ß-Amyloid peptide, Abs/Em=503/528 nm. Hilyte™ Fluor 488 labeled Aß (1-42) has a brighter intensity than FAM-labeled Aß (1-42).

Specifications

Chemistry
Sequence one letter code
  • HiLyte Fluor™ 488-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Sequence three letter code
  • Hilyte™ Fluor488-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-OH
Molecular Mass/ Weight
  • 4870.8
Properties
Absorbance (nm)
  • 503
Emission (nm)
  • 528
Modification
Conjugation type
  • Fluorescent dyes
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • ≥ 95%
Storage & stability
Form
  • Lyophilized
Activity
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human
Codes
Code Nacres
  • NA.26

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Citations

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  • et al

Bone Marrow-Derived Macrophages from AβPP/PS1 Mice are Sensitized to the Effects of Inflammatory Stimuli

J Alzheimers Dis . 2014 Oct 03 ; 44(3) 949 | DOI : 10.3233/JAD-142076

  • A. Minogue
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Simultaneous measurement of a range of particle sizes during Aβ1–42 fibrillogenesis quantified using fluorescence correlation spectroscopy

Biochem Biophys Res Commun. . 2014 Mar 30 ; 448(2) 195 | DOI : 10.1016/j.bbrc.2014.04.088

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Autophagy is involved in oligodendroglial precursor-mediated clearance of amyloid peptide

Mol Neurodegener . 2013 Aug 10 ; 8 22 | DOI : 10.1186/1750-1326-8-27

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Reduction of Synaptojanin 1 Accelerates Aβ Clearance and Attenuates Cognitive Deterioration in an Alzheimer Mouse Model

J Biol Chem. . 2013 Nov 01 ; 288(44) 32050 | DOI : 10.1074/jbc.M113.504365

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Massive gliosis induced by interleukin-6 suppresses Aβ deposition in vivo: evidence against inflammation as a driving force for amyloid deposition

FASEB J . 2009 Oct 13 ; 24(2) 548 | DOI : https://doi.org/10.1096/fj.09-141754

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Simple in vitro assays to identify amyloid-β aggregation blockers for Alzheimer's disease therapy

J Alzheimers Dis . 2009 Nov 10 ; 19(4) 1359 | DOI : 10.3233/JAD-2010-1331

  • JP. Guo
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The NALP3 inflammasome is involved in the innate immune response to amyloid-β

Nat Immunol. . 2008 Jul 11 ; 9(8) 857 | DOI : 10.1038/ni.1636

  • A. Halle
  • et al

Microglial Dysfunction and Defective β-Amyloid Clearance Pathways in Aging Alzheimer's Disease Mice

J Neurosci. . 2008 Aug 13 ; 28(33) 8354 | DOI : 10.1523/JNEUROSCI.0616-08.2008

  • S. Hickman
  • et al

LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-β peptide in a blood–brain barrier in vitro model

Neurobiol Dis. . 2008 Apr 01 ; 30(1) 94 | DOI : 10.1016/j.nbd.2007.12.005

  • B. Nazer
  • et al

Detection of Alzheimer’s amyloid beta aggregation by capturing molecular trails of individual assemblies

Biochem Biophys Res Commun . 2008 Dec 12 ; 377(2) 725 | DOI : 10.1016/j.bbrc.2008.10.072

  • M. Vestergaard
  • et al

Direct Observations of Amyloid β Self-Assembly in Live Cells Provide Insights into Differences in the Kinetics of Aβ(1–40) and Aβ(1–42) Aggregation

Chem Biol. . 2014 Jun 19 ; 21(6) 732 | DOI : 10.1016/j.chembiol.2014.03.014

  • EK. Esbjörner
  • et al

Rare Individual Amyloid-β Oligomers Act on Astrocytes to Initiate Neuronal Damage

Biochemistry. . 2014 Apr 09 ; 53(15) 2442 | DOI : 10.1021/bi401606f

  • P. Narayan
  • et al

Direct Observations of Amyloid β Self-Assembly in Live Cells Provide Insights into Differences in the Kinetics of Aβ (1–40) and Aβ (1–42) Aggregation.

Chem Biol . 2014 Jun 19 ; 21(6) 732 | DOI : 10.1016/j.chembiol.2014.03.014

  • EK. Esbjörner