Recombinant Rat Oncomodulin (Ocm) is produced using a yeast expression system, which appears to deliver high-quality protein expression. The full-length mature protein carries an N-terminal 10xHis-tag that makes purification and detection more straightforward. SDS-PAGE analysis confirms the recombinant protein achieves greater than 90% purity. This product is intended strictly for research purposes and may serve as a reliable tool across different experimental setups.
Oncomodulin (Ocm) is a calcium-binding protein that seems to play a crucial role in cellular processes where calcium regulation matters. Its structure relates closely to calmodulin, making it particularly significant for studies that focus on calcium signaling pathways. The protein's involvement in cellular growth and differentiation likely makes it important for research exploring cellular development and regeneration.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Calcium-Binding Protein Interaction Studies
Researchers might use this recombinant rat oncomodulin to investigate calcium-dependent protein-protein interactions in laboratory settings. The N-terminal 10xHis tag allows for protein purification and immobilization during pull-down assays when searching for potential binding partners. Scientists can explore how calcium availability influences oncomodulin's interactions with other cellular proteins through co-immunoprecipitation or surface plasmon resonance approaches. The yeast expression system likely provides properly folded protein that works well for biochemical characterization of these interactions.
2. Antibody Development and Validation
This recombinant protein may serve as an excellent antigen for creating specific antibodies against rat oncomodulin. The >90% purity level appears sufficient for immunization protocols during antibody production. His-tagged protein can be applied in ELISA-based screening to identify high-affinity antibodies and confirm their specificity. This application supports developing research tools for studying oncomodulin expression and localization in rat tissues and cell lines.
3. Biochemical Characterization of Calcium-Binding Properties
The purified recombinant oncomodulin offers opportunities to study its calcium-binding kinetics and thermodynamics through methods like isothermal titration calorimetry or fluorescence spectroscopy. Scientists can determine binding constants, stoichiometry, and conformational changes that occur upon calcium binding. The His tag makes protein purification and concentration determination simpler for quantitative biochemical assays. These studies may provide fundamental insights into oncomodulin's molecular properties and calcium-sensing mechanisms.
4. Comparative Species Analysis
This rat oncomodulin can work alongside oncomodulin proteins from other species during comparative biochemical studies. Scientists might examine species-specific differences in calcium sensitivity, protein stability, or binding partner preferences through parallel in vitro assays. The standardized expression system and His tag purification approach appears to ensure consistent protein quality for reliable comparative analysis. Such studies could contribute to understanding evolutionary conservation and divergence of oncomodulin function across mammalian species.
