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 (25–35), 11 amino-acid residues.
Linear reference chainView full size
Reference sequence11 residues
GSNKGAIIGLM

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

PL-BET-028 Beta-amyloid peptides

Beta-Amyloid (25–35)

$79.99

Human amyloid-beta fragment spanning Aβ residues 25–35, comprising 11 amino acids for laboratory studies of peptide sequence, fragment boundaries, and molecular association.

In stock

SKU: PL-BET-028 Category:

Technical identity

Catalog ID
PL-BET-028
Construct
Human APP770 residues 696–706; beta-amyloid-relative numbering 25–35
Reference sequence
GSNKGAIIGLM
Calculated reference mass
1060.28 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 (25–35) is a 11-amino-acid peptide corresponding to residues 25–35 of the human amyloid-beta (Aβ) sequence. These positions map to residues 696–706 of amyloid precursor protein isoform APP770. Sequence reference: UniProt P05067.

Research context

This fragment begins at glycine 25 and ends at methionine 35 in Aβ numbering. These defined boundaries isolate a particular portion of the parent sequence for comparisons with longer Aβ chains and overlapping fragments. The reference sequence represents the unmodified amino acids between those boundaries.

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(25–35) 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-028
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 11 amino acids
  • Reference region: Human APP770 residues 696–706; beta-amyloid-relative numbering 25–35
  • Calculated average molecular mass: 1,060.28 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

GSNKGAIIGLM

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

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