Aβ1-14-εK-KKK-MvF5 Th integrates an Aβ(1-14) fragment with additional lysine-rich extensions and an MvF5 tag for tracking aggregation behavior. Researchers use it to monitor early oligomer formation, peptide-membrane interactions, and sequence-driven fibrillization. The construct provides strong spectroscopic handles for real-time assays. Applications include amyloid-mechanism research and aggregation-modulator screening.
CAT No: Z10-101-227
Aβ1-14-εK-KKK-MvF5 Th is a synthetic peptide derivative engineered to incorporate key residues from the N-terminal region of the amyloid beta (Aβ) peptide, with site-specific modifications and appended functional sequences. Its design reflects a strategic combination of the Aβ1-14 epitope, a lysine-rich linker, and the MvF5 Th moiety, enabling advanced studies in amyloid biology, protein aggregation mechanisms, and peptide-based molecular engineering. The unique sequence architecture and chemical features of this peptide make it a valuable tool for researchers investigating the structural and functional dynamics of amyloidogenic pathways, as well as for applications requiring precise peptide conjugation and interaction profiling.
Peptide aggregation research: The compound is particularly well-suited for in vitro studies of amyloidogenic processes, serving as a model system for examining the early-stage aggregation of Aβ-derived sequences. Its defined N-terminal region, coupled with engineered linkers, allows researchers to dissect the molecular determinants of oligomerization and fibril formation. By enabling controlled aggregation assays, the peptide facilitates the elucidation of sequence-specific contributions to amyloid assembly, supporting efforts to map the biophysical landscape of protein misfolding and aggregation disorders at a mechanistic level.
Epitope mapping and antibody characterization: The inclusion of the Aβ1-14 segment in this peptide provides a robust platform for immunological studies, particularly for mapping antibody epitopes and assessing the specificity of anti-amyloid antibodies. Researchers can employ the peptide in binding assays such as ELISA, surface plasmon resonance, or immunoprecipitation to evaluate antibody recognition patterns, affinity, and cross-reactivity. Such applications are instrumental in the development and validation of novel immunoreagents targeting amyloid structures or in the optimization of diagnostic tools for amyloid-related research.
Peptide conjugation and functionalization: The εK-KKK linker and the MvF5 Th domain offer versatile chemical handles for site-specific conjugation, allowing for the attachment of fluorescent probes, affinity tags, or other functional moieties. This property enables the design of customized molecular probes for imaging, tracking, or pull-down assays. The peptide's modular architecture thus supports advanced labeling strategies, facilitating the study of peptide localization, trafficking, and interaction dynamics within complex biological systems.
Protein-protein interaction studies: The engineered sequence can be used as a bait or target in assays designed to probe interactions between amyloidogenic peptides and cellular binding partners. Its defined structure and modifiable regions make it suitable for pull-down experiments, crosslinking studies, and biophysical analyses aimed at characterizing the binding interfaces and affinities of amyloid-related complexes. These applications contribute to a deeper understanding of the molecular interactions underpinning amyloid biology and inform the design of modulators for research use.
Peptide-based screening platforms: The compound's stability and specificity render it a suitable component for high-throughput screening platforms targeting amyloid aggregation or disruption. Researchers can integrate the peptide into assay systems to identify small molecules, peptides, or proteins that modulate its aggregation behavior or binding properties. Such platforms are valuable for the discovery and validation of research tools and molecular probes relevant to neurodegenerative disease mechanisms and amyloid research.
Collectively, these application directions highlight the scientific versatility and technical value of this peptide in advancing research across amyloid aggregation, immunological profiling, bioconjugation, interaction mapping, and screening methodologies. Its precisely engineered sequence and functional domains enable a range of experimental approaches that support the elucidation of amyloid-related processes and the development of innovative research tools in the field of peptide science.
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