IN VITRO LABORATORY RESEARCH ONLYQualified research organizations · No human or animal administration

Molecular structure

2D reference
Sequence-derived 2D chemical structure of Beta-Amyloid (1–42), E22Q, 42 amino-acid residues. Q22 is highlighted in gold.
E22Q substitution · Gln22View full size
Reference sequence42 residues
DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVVIA

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

PL-BET-038 Beta-amyloid peptides

Beta-Amyloid (1–42), E22Q

$24.99

Human Aβ42 peptide with the E22Q substitution, comprising 42 amino acids for comparative laboratory studies of amyloid sequence variants and molecular assembly.

In stock

SKU: PL-BET-038 Category:

Technical identity

Catalog ID
PL-BET-038
Construct
Human Aβ1–42 reference chain with E22Q substitution
Reference sequence
DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVVIA
Calculated reference mass
4513.11 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
E22Q substitution relative to Aβ1–42

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

Documentation

For specification, analytical-record or handling questions, contact our team with the product name or catalog ID.

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

Description

Beta-Amyloid (1–42), E22Q is a 42-amino-acid peptide corresponding to residues 1–42 of the human amyloid-beta (Aβ) sequence. These positions map to residues 672–713 of amyloid precursor protein isoform APP770. Sequence reference: UniProt P05067.

Research context

The E22Q substitution replaces glutamic acid with glutamine at Aβ position 22, corresponding to APP770 position 693. The remaining residues follow the Aβ(1–42) reference sequence. This defined substitution provides a focused comparison with the unmodified Aβ42 chain in studies of sequence-dependent molecular association and conformation.

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 E22Q sequence variant with unmodified Aβ42.
  • Investigating sequence-dependent peptide association and conformational behavior.
  • Characterizing oligomeric or fibrillar assemblies in defined in vitro research systems.

Molecular identity

  • Catalog ID: PL-BET-038
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 42 amino acids
  • Reference region: Human Aβ1–42 reference chain with E22Q substitution
  • Calculated average molecular mass: 4,513.11 Da for the free-acid reference chain with the stated substitution
  • Sequence modification: E22Q substitution

Reference sequence

DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVVIA

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