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), D7H, 42 amino-acid residues. H7 is highlighted in gold.
D7H substitution · His7View full size
Reference sequence42 residues
DAEFRHHSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

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

PL-BET-035 Beta-amyloid peptides

Beta-Amyloid (1–42), D7H

$139.99

Human Aβ42 peptide with the D7H substitution, comprising 42 amino acids for comparative laboratory studies of amyloid sequence variants and molecular assembly.

In stock

SKU: PL-BET-035 Category:

Technical identity

Catalog ID
PL-BET-035
Construct
Human Aβ1–42 reference chain with D7H substitution
Reference sequence
DAEFRHHSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Calculated reference mass
4536.15 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
D7H 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), D7H 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 D7H substitution replaces aspartic acid with histidine at Aβ position 7, corresponding to APP770 position 678. 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 D7H 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-035
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 42 amino acids
  • Reference region: Human Aβ1–42 reference chain with D7H substitution
  • Calculated average molecular mass: 4,536.15 Da for the free-acid reference chain with the stated substitution
  • Sequence modification: D7H substitution

Reference sequence

DAEFRHHSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

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