UBX domain-containing protein 11 (447-460)

UBX domain-containing protein 11 (447-460) is a synthetic peptide fragment derived from the C-terminal region of the human UBX domain-containing protein 11, a member of the ubiquitin regulatory X (UBX) domain-containing protein family. This peptide encompasses amino acids 447 to 460, corresponding to a segment implicated in protein-protein interactions and cellular regulatory processes related to ubiquitin-mediated pathways. As a chemically defined peptide, it serves as a valuable tool for dissecting the molecular functions of UBX domain-containing proteins, which are recognized for their roles in modulating ubiquitin-dependent proteostasis and protein quality control in eukaryotic cells. The sequence specificity and structural relevance of this fragment provide researchers with a focused means to interrogate the biochemical and functional properties of the parent protein in controlled experimental settings.

Protein interaction studies: The peptide is particularly useful in mapping interaction sites within the UBX domain-containing protein 11 and its binding partners. By employing this defined fragment in binding assays such as surface plasmon resonance or co-immunoprecipitation, researchers can delineate the critical residues involved in the recognition and association with ubiquitin or other regulatory proteins. This approach enables the identification of interaction motifs and the characterization of molecular determinants essential for protein-protein communication within ubiquitin signaling pathways.

Peptide-based inhibitor design: The defined sequence of the 447-460 fragment provides a template for rational design of peptide-based inhibitors or mimetics targeting the interaction interfaces of UBX domain-containing proteins. By evaluating the binding affinity and inhibitory properties of this peptide in vitro, scientists can develop structure-activity relationship models that inform the development of modulators capable of disrupting aberrant protein interactions implicated in proteostasis dysregulation. Such studies advance the broader field of targeted protein modulation using synthetic peptides.

Structural biology applications: The fragment serves as an ideal candidate for structural investigations, including solution-state nuclear magnetic resonance (NMR) and X-ray crystallography. Incorporation of the peptide into structural studies aids in elucidating the conformational dynamics of the UBX domain and its interaction surfaces. Insights gained from these analyses contribute to a detailed understanding of the three-dimensional organization and flexibility of UBX domain-containing protein 11, informing hypotheses regarding its regulatory mechanisms.

Antibody generation and epitope mapping: The synthetic peptide corresponding to amino acids 447-460 can be employed as an immunogen for the production of sequence-specific antibodies. Such antibodies are instrumental in detecting the native protein in cellular extracts, facilitating studies of protein localization, expression levels, and post-translational modifications. Additionally, the peptide is valuable for epitope mapping experiments, enabling researchers to pinpoint antibody binding sites and validate the specificity of immunological reagents used in proteomic workflows.

Assay development and validation: The availability of a well-defined peptide standard supports the development and optimization of analytical assays, such as enzyme-linked immunosorbent assays (ELISA) or mass spectrometry-based quantification methods. Use of the 447-460 fragment as a calibrator or positive control enhances the accuracy and reproducibility of assays designed to monitor UBX domain-containing protein 11 or related pathway components. This application underpins robust quantitative and qualitative analyses in both basic and applied biochemical research.

1. Effect of Short-Term Desiccation, Recovery Time, and CAPA-PVK Neuropeptide on the Immune System of the Burying Beetle Nicrophorus vespilloides

2. TMEM16F and dynamins control expansive plasma membrane reservoirs

3. Constitutive and inflammation-dependent antimicrobial peptides produced by epithelium are differentially processed and inactivated by the commensal Finegoldia magna and the pathogen Streptococcus pyogenes

4. Cationic cell-penetrating peptides are potent furin inhibitors

5. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)