Pure Lab.RESEARCH MATERIALS
IN VITRO LABORATORY RESEARCH ONLYQualified research organizations · No human or animal administration

Molecular structure

2D reference
Sequence-derived 2D chemical structure of Beta-Amyloid (1–43), 43 amino-acid residues.
Linear reference chainView full size
Reference sequence43 residues
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT

Sequence-derived chemical connectivity. Free N terminus and C-terminal acid; no specific 3D fold is implied.

PL-BET-003 Beta-amyloid peptides

Beta-Amyloid (1–43)

$119.99

Human amyloid-beta fragment spanning Aβ residues 1–43, comprising 43 amino acids for laboratory studies of peptide sequence, fragment boundaries, and molecular association.

In stock

SKU: PL-BET-003 Category:

Technical identity

Catalog ID
PL-BET-003
Construct
Human APP770 residues 672–714; beta-amyloid-relative numbering 1–43
Reference sequence
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT
Calculated reference mass
4615.20 Da — calculated average mass of the unmodified free-acid chain; not a measured result. Tags, termini, modifications, counterions and disulfides change the actual mass.
Reference modifications
Unmodified reference chain

Reference identity: UniProt P05067. Calculated mass describes the reference chain and does not replace a measured lot result.

Documentation

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For qualified organizational in vitro research only. Purchasing access is available to approved research organizations.

Description

Beta-Amyloid (1–43) is a 43-amino-acid peptide corresponding to residues 1–43 of the human amyloid-beta (Aβ) sequence. These positions map to residues 672–714 of amyloid precursor protein isoform APP770. Sequence reference: UniProt P05067.

Research context

This sequence extends Aβ42 by one C-terminal threonine residue. It defines a 43-residue chain for comparisons among Aβ species with different C-terminal boundaries. Such comparisons examine how a small change in peptide length can alter the chemical context of the terminus and influence molecular association in a defined experimental system. It includes the KLVFF segment at Aβ residues 16–20, a sequence examined in studies of amyloid molecular recognition and assembly. Molecular-recognition reference.

Amyloid-beta research examines the relationship between peptide sequence and the development of oligomeric and fibrillar assemblies. A defined sequence and terminal boundary allow researchers to separate questions about molecular identity from the effects of the experimental environment. Observed assembly depends on the particular chain and the conditions used for its characterization. Research reference.

Research applications

  • Comparing the Aβ(1–43) sequence with longer or overlapping amyloid-beta chains.
  • Mapping sequence contributions to molecular recognition and peptide association.
  • Analytical and biophysical characterization of a defined amyloid-beta fragment.

Molecular identity

  • Catalog ID: PL-BET-003
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 43 amino acids
  • Reference region: Human APP770 residues 672–714; beta-amyloid-relative numbering 1–43
  • Calculated average molecular mass: 4,615.20 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT

For in vitro laboratory research only. Not for human or animal administration.

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