Cy5-Amyloid β Peptide (42-1) (human) features a Cy5 fluorophore conjugated to the Aβ(42-1) sequence, enabling visualization of aggregation and binding events. The peptide preserves the hydrophobic and β-structure-forming motifs of the parent Aβ region. Researchers track fibrillization kinetics and interactions with membranes or chaperones using fluorescence methods. Applications include aggregation-mechanism studies, inhibitor screening, and supramolecular-assembly research.
CAT No: Z10-101-191
Cy5-Amyloid β Peptide (42-1)(human) is a synthetic peptide conjugated with the Cy5 fluorescent dye, specifically engineered for advanced research into amyloid β aggregation and its molecular dynamics. This reverse sequence peptide, corresponding to the human amyloid β (Aβ) residues 42 to 1, is widely utilized in fluorescence-based studies due to its robust photostability and high quantum yield, making it a powerful tool for monitoring peptide behavior in real time. The Cy5 label allows for sensitive detection and quantification, facilitating its integration into a variety of fluorescence imaging and spectroscopy platforms. By mimicking the reverse sequence of the amyloid β peptide, Cy5-Amyloid β Peptide (42-1)(human) serves as a valuable negative control in aggregation studies, helping to distinguish specific interactions from non-specific background signals. Its design and properties support a broad spectrum of applications in neurodegenerative disease research, molecular interaction analysis, and high-throughput screening protocols.
Neurodegenerative Disease Mechanism Research: Cy5-Amyloid β Peptide (42-1)(human) is instrumental in dissecting the molecular mechanisms underlying amyloid β aggregation, a hallmark of neurodegenerative disorders such as Alzheimer's disease. Researchers employ this labeled peptide in in vitro aggregation assays, where its fluorescence enables real-time monitoring of aggregation kinetics and the formation of oligomeric or fibrillar structures. The reverse sequence acts as a negative control, allowing scientists to validate the specificity of aggregation pathways and to differentiate between sequence-dependent and non-sequence-dependent interactions. By providing a reliable means to track peptide behavior, this tool enhances the understanding of amyloidogenic processes and supports the development of potential aggregation inhibitors.
Protein-Protein Interaction Studies: The Cy5-labeled Aβ (42-1) peptide is extensively used to probe protein-protein interactions relevant to amyloid pathology. In fluorescence resonance energy transfer (FRET) and fluorescence correlation spectroscopy (FCS) experiments, the Cy5 tag enables precise detection of interactions between amyloid peptides and other biomolecules, such as chaperones, enzymes, or small-molecule modulators. By serving as a control that does not undergo typical aggregation, this peptide helps researchers discern specific binding events and elucidate the molecular determinants of amyloid β recognition and assembly. These insights are critical for mapping the interaction networks that govern amyloid biology.
High-Content Screening Applications: In drug discovery and screening platforms, Cy5-Amyloid β Peptide (42-1)(human) is incorporated into high-content assays designed to identify compounds that modulate amyloid aggregation or disrupt pathological interactions. The strong fluorescence signal of Cy5 allows for sensitive, automated readouts in microplate-based formats, supporting the rapid evaluation of large compound libraries. By using the reverse sequence peptide as a baseline, researchers can control for non-specific fluorescence changes and improve the reliability of screening results. This application accelerates the identification of lead molecules with potential therapeutic relevance.
Cellular Uptake and Trafficking Studies: Investigators leverage the fluorescent properties of Cy5-Aβ (42-1) to study peptide uptake, intracellular localization, and trafficking within cellular models. The reverse sequence confers minimal aggregation propensity, enabling clear visualization of peptide distribution without confounding effects from fibril formation. By tracking the Cy5 signal through confocal microscopy or flow cytometry, researchers can assess cellular internalization pathways, peptide stability, and subcellular compartmentalization. These studies contribute to a deeper understanding of peptide transport mechanisms and cellular responses to amyloidogenic species.
Biophysical Characterization and Method Validation: Cy5-Amyloid β Peptide (42-1)(human) is a preferred standard for validating and calibrating fluorescence-based analytical techniques, such as single-molecule spectroscopy, fluorescence lifetime imaging microscopy (FLIM), and flow cytometry. Its defined sequence and consistent labeling facilitate reproducibility in experimental protocols, allowing researchers to optimize detection parameters and quantify assay sensitivity. By serving as a non-aggregating control, it ensures that observed fluorescence signals are attributable to specific experimental variables rather than unintended peptide aggregation or degradation. This role is essential for establishing assay robustness and for benchmarking new methodologies in amyloid research.
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