Peptides

[Gln22]-beta-Amyloid (1-42), Dutch mutation - 0.5 mg

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  • Cat.Number : AS-62142
  • Availability :
    In stock

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This peptide is a naturally occurring mutant form of the wild type (WT) beta-Amyloid 1 to 42 peptide. The E22Q "Dutch" mutant, also known as HCHWA-D, is caused by a point mutation in the beta-Amyloid encoding gene, with Glu replaced by Gln at position 22. Dutch E22Q mutation in beta-Amyloid causes familial cerebrovascular amyloidosis with abundant diffused amyloid plaque deposits. E22Q mutant and WT peptides are both stable in "collapsed coil" conformations. The E22Q fibrils are more toxic for vascular cells than the WT fibrils.

Specifications

Chemistry
Sequence one letter code
  • DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVVIA
Sequence three letter code
  • H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Gln-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala-OH
Molecular Formula
  • C203H312N56O59S1
Molecular Mass/ Weight
  • 4513.4
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human

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References

Early-onset and Robust Cerebral Microvascular Accumulation of Amyloid β-Protein in Transgenic Mice Expressing Low Levels of a Vasculotropic Dutch/Iowa Mutant Form of Amyloid β-Protein Precursor

J Biol Chem . 2004 May 01 ; 279(19) 20296 | DOI : https://doi.org/10.1074/jbc.M312946200

  • J. Davis
  • et al

Vitamin E But Not 17β-Estradiol Protects against Vascular Toxicity Induced by β-Amyloid Wild Type and the Dutch Amyloid Variant

Neurosci. . 2002 Apr 15 ; 22(8) 3081 | DOI : https://doi.org/10.1523/JNEUROSCI.22-08-03081.2002

  • F. Muñoz
  • et al

Probing the Origins of Increased Activity of the E22Q “Dutch” Mutant Alzheimer's β-Amyloid Peptide

Biophys J . 2001 Aug 01 ; 81(2) 697 | DOI : https://doi.org/10.1016/S0006-3495(01)75734-7

  • F. Massi
  • J. Straub