E3 ubiquitin-protein ligase UBR4
E3 ubiquitin-protein ligase UBR4 (329-337) is a synthetic peptide fragment derived from the UBR4 protein, a member of the E3 ubiquitin ligase family involved in the N-end rule pathway of protein degradation. This short peptide sequence corresponds to residues 329 through 337 of the UBR4 protein, which plays a crucial role in recognizing and targeting specific substrates for ubiquitination and subsequent proteasomal degradation. The availability of this defined peptide segment enables researchers to investigate the structural and functional aspects of substrate recognition, binding specificity, and the broader regulatory mechanisms orchestrated by UBR4 within cellular protein quality control systems.
Ubiquitin pathway research: As a peptide fragment from the UBR4 protein, this compound serves as a valuable tool for dissecting the molecular details of the ubiquitin-proteasome system. Researchers can utilize it to map interaction domains or to screen for binding partners that specifically recognize the 329-337 region, thereby elucidating the selectivity and regulatory checkpoints of E3 ligase-mediated substrate processing. Such studies contribute to a deeper understanding of how protein homeostasis is maintained in eukaryotic cells.
Protein-protein interaction studies: The defined sequence of the UBR4 (329-337) peptide enables its use in in vitro binding assays, including peptide pull-down experiments and surface plasmon resonance analyses. By immobilizing the peptide or introducing it as a competitor, scientists can assess the affinity and specificity of interacting proteins, such as substrate adaptors, regulatory cofactors, or other components of the ubiquitin ligase complex. These insights are essential for mapping critical contact points and for developing hypotheses about the assembly and regulation of multi-protein complexes involved in ubiquitination.
Antibody generation and epitope mapping: The synthetic peptide corresponding to residues 329-337 of UBR4 can be employed as an immunogen for the production of sequence-specific antibodies. Such antibodies are invaluable for detecting UBR4 or its processed forms in various biological samples using immunoblotting, immunoprecipitation, or immunofluorescence techniques. Additionally, the peptide can be used to map antibody binding sites, aiding in the characterization and validation of antibody specificity during assay development.
Peptide-based assay development: The UBR4 (329-337) fragment offers a defined substrate for the design and optimization of biochemical assays aimed at monitoring E3 ligase activity, substrate recognition, or inhibitor screening. By incorporating the peptide into fluorescence polarization, ELISA, or FRET-based platforms, researchers can quantitatively assess interactions and modulatory effects in a controlled and reproducible manner. Such assays are instrumental in mechanistic studies and in the identification of small-molecule modulators targeting the ubiquitin-proteasome pathway.
Structural and conformational analysis: The short, well-defined nature of the 329-337 peptide makes it suitable for biophysical investigations, including NMR spectroscopy and crystallography, to probe its secondary structure or to model its interaction with binding partners. These structural insights can inform rational design strategies for mimetics or inhibitors, and enhance our understanding of how specific sequence motifs contribute to the functional specificity of E3 ubiquitin ligases.
2. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
3. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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