Description
Beta-Amyloid (1–42), E22K 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 E22K substitution replaces glutamic acid with lysine 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 E22K 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-039
- Product type: Peptide
- Reference species: Human (Homo sapiens)
- Sequence length: 42 amino acids
- Reference region: Human Aβ1–42 reference chain with E22K substitution
- Calculated average molecular mass: 4,513.15 Da for the free-acid reference chain with the stated substitution
- Sequence modification: E22K substitution
Reference sequence
DAEFRHDSGYEVHHQKLVFFAKDVGSNKGAIIGLMVGGVVIA
For in vitro laboratory research only. Not for human or animal administration.