UBI29-41 is a fragment of ubiquitin containing residues that form a flexible yet structured recognition epitope. The sequence includes hydrophobic and charged side chains that participate in protein-protein interactions. Researchers use it to study ubiquitin-binding domains and interaction hot spots. Applications include PPI mapping, motif-function analysis, and peptide-based probe development.
CAT No: R2779
UBI29-41 is a synthetic peptide fragment derived from the C-terminal region of human ubiquitin, comprising residues 29 through 41. As a well-defined peptide sequence, it serves as a valuable molecular tool for investigating the structure and function of ubiquitin and its related biochemical pathways. The sequence represents a functionally significant domain implicated in protein-protein interactions, post-translational modifications, and the regulation of cellular processes. Researchers utilize this fragment to dissect the mechanistic aspects of ubiquitin signaling, to probe the specificity of ubiquitin-binding proteins, and to support studies in proteostasis and cellular homeostasis. Its defined nature and biological relevance position it as a critical reagent for advancing peptide-based research in molecular and cellular biology.
Protein-Protein Interaction Studies: UBI29-41 is frequently employed in the analysis of protein-protein interactions involving ubiquitin and its binding partners. By providing a discrete segment of the ubiquitin molecule, the peptide allows researchers to map interaction interfaces and to determine the binding specificity of ubiquitin-interacting motifs (UIMs) and other recognition domains. This approach is instrumental in elucidating the molecular determinants of ubiquitin recognition, contributing to a deeper understanding of how ubiquitin-mediated signaling is orchestrated within the cell.
Enzyme Substrate Profiling: The peptide serves as a model substrate for studying the activity and specificity of deubiquitinating enzymes (DUBs) and ubiquitin-processing proteases. By exposing the C-terminal region, which is critical for many enzymatic modifications, UBI29-41 enables detailed kinetic and mechanistic analyses of DUBs, facilitating the identification of substrate preferences and catalytic mechanisms. Such studies are essential for characterizing enzyme function and for screening potential modulators of ubiquitin-dependent pathways.
Peptide-Based Inhibitor Design: UBI29-41 provides a structural template for the rational design and optimization of peptide-based inhibitors targeting ubiquitin-binding proteins or enzymes involved in ubiquitin signaling. Researchers utilize the sequence to develop competitive inhibitors or molecular probes that can modulate specific protein interactions or enzymatic activities. This application supports the development of chemical biology tools for dissecting signaling networks and for validating potential drug targets in preclinical research.
Structural Biology Applications: The defined sequence of UBI29-41 makes it an ideal candidate for structural studies using techniques such as nuclear magnetic resonance (NMR) spectroscopy or X-ray crystallography. By incorporating the peptide into model systems, scientists can investigate conformational dynamics, secondary structure propensities, and the influence of post-translational modifications on peptide folding and interaction. These insights are invaluable for understanding the biophysical properties of ubiquitin fragments and their roles in cellular regulation.
Analytical Assay Development: The peptide is also utilized in the development and validation of analytical assays designed to detect, quantify, or characterize ubiquitin fragments in complex biological samples. Its well-defined sequence and known properties facilitate the calibration of mass spectrometry-based methods, immunoassays, and other detection platforms. These applications are critical for advancing quantitative proteomics and for supporting high-throughput screening efforts in ubiquitin research.
Through these diverse applications, UBI29-41 serves as a foundational tool for peptide research, advancing the molecular understanding of ubiquitin biology and enabling the development of innovative experimental approaches in the life sciences. Its versatility and scientific relevance make it a preferred choice for researchers seeking to explore the complexities of protein modification and cellular signaling pathways.
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