Peptides

Beta-Amyloid (1-39) Peptide

185.00
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  • Cat.Number : AS-24295
  • Availability :
    In production

Size

Quantity

A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-39) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

Specifications

Chemistry
Sequence one letter code
  • DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGV
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-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-OH
CAS registry number
  • 115427-62-8
Molecular Formula
  • C189H286N52O57S
Molecular Mass/ Weight
  • 4231
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human
Codes
Code Nacres
  • NA.26

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Citations

Microchip electrophoresis profiling of Aβ peptides in the cerebrospinal fluid of patients with Alzheimer’s disease.

Anal Chem . 2010 Sep 15 ; 82(18) 7611 | DOI : 10.1021/ac101337n

  • M. Reza
  • et al

Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons.

Biophys J 70, 296. . 1996 Jan 01 ; 70(1) 296 | DOI : 10.1016/S0006-3495(96)79570-X

  • TA. Good
  • et al

Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity.

Biochem . 1999 Mar 23 ; 38(12) 3570 | DOI : 10.1021/bi982119e

  • MM. Pallitto
  • et al

A strategy for designing inhibitors of β-amyloid toxicity.

J Biol Chem . 1996 Nov 22 ; 271(47) 29525 | DOI : 10.1074/jbc.271.47.29525

  • J. Ghanta
  • et al