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N3-Lys-Amyloid Beta 1-42 Peptide is derived from the amyloid-beta sequence generated from human amyloid-beta precursor protein (APP). The canonical Aβ region is publicly curated within human APP UniProtKB entry P05067.
Amyloid Beta Research Peptides
Amyloid-beta peptides are central research reagents in studies of peptide aggregation, amyloid fibril formation, membrane interactions, proteolytic processing, antibody recognition, and analytical assay development. Aβ1-40 and Aβ1-42 are the two most widely studied C-terminal forms.
Aβ1-42 contains two additional C-terminal residues relative to Aβ1-40 and generally displays stronger aggregation propensity under many experimental conditions. Sequence, concentration, solvent history, pre-treatment, and incubation conditions can all strongly affect aggregation state.
Aβ1-42 Parent Sequence
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
N-Terminal Azido-Lysine Handle
LT8744 contains the complete Aβ1-42 sequence preceded by an added Lys(N3) residue. The azide functionality provides a site for click-chemistry conjugation while leaving all 42 residues of the canonical Aβ sequence present in the construct.
The added lysine is not part of native Aβ1-42 and can influence physicochemical behavior; application-specific validation is recommended.
Potential Research Applications
- Amyloid aggregation studies
- LC-MS analytical methods
- Antibody binding assays
- Peptide-protein interaction studies
- Fluorescent or chemical conjugation
- Reference-standard development
For aggregation-sensitive studies, peptide handling and pre-treatment procedures should be standardized across experiments.
References
UniProt Consortium APP - Amyloid-beta precursor protein - Homo sapiens. UniProtKB P05067.
Public source / publication Related LifeTein Services
Custom Peptide Synthesis
Fluorescent Peptide Labeling
Peptide Click Chemistry and Conjugation
Peptide Carrier Protein Conjugation
Research Use Only. Not for human, diagnostic, clinical, or therapeutic use.
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