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.
Rat Ocm is a calcium-binding protein belonging to the EF-hand superfamily that requires precise folding and proper EF-hand domain formation for its calcium-binding functionality. The yeast expression system provides a eukaryotic environment that supports proper protein folding, disulfide bond formation, and post-translational modifications, significantly increasing the probability of correct folding compared to bacterial systems. The N-terminal 10xHis tag is relatively small and unlikely to interfere with the protein's calcium-binding domains. However, experimental validation remains essential to confirm both structural integrity and functional calcium-binding activity.
1. Calcium-Binding Protein Interaction Studies
This application's reliability depends entirely on proper folding validation. Calcium-dependent protein interactions require precise tertiary structure formation of EF-hand domains. If correctly folded and calcium-binding competent (verified), the protein is highly suitable for studying physiological interaction partners in calcium signaling pathways. If misfolded/unverified, there is high risk of non-specific binding or interaction failure, making results biologically misleading.
2. Antibody Development and Validation
Antibody development primarily relies on antigenic sequence recognition rather than functional folding. If correctly folded (verified), the protein excels for generating conformation-sensitive antibodies that recognize native oncomodulin epitopes. If misfolded/unverified, it remains highly suitable for producing antibodies against linear epitopes, which are still valuable for detection applications.
3. Biochemical Characterization of Calcium-Binding Properties
These studies are essential for determining folding status and functional competence. If correctly folded and active (verified), characterization provides reliable data on calcium-binding kinetics, stoichiometry, and conformational changes. If misfolded/unverified, analysis yields physical property data, but calcium-binding assays will not reflect native activity.
4. Comparative Species Analysis
Meaningful comparative studies require native protein conformation and functional activity. If correctly folded and calcium-binding competent (verified), the protein enables valid functional comparisons with oncomodulin orthologs from other species. If misfolded/unverified, comparative analyses would yield misleading results about evolutionary relationships and functional differences.
Final Recommendation & Action Plan
The yeast expression system provides favorable eukaryotic folding conditions for this calcium-binding protein, but experimental validation of structural integrity and calcium-binding activity is essential before reliable use in functional studies. Begin with Application 3 (Biochemical Characterization) to assess folding quality through circular dichroism spectroscopy (EF-hand structure analysis), size-exclusion chromatography, and validate calcium-binding activity using isothermal titration calorimetry or fluorescence-based assays. If correct folding and calcium-binding functionality are verified, proceed confidently with Applications 1 and 4 for interaction studies and comparative analyses. Application 2 (antibody development) can proceed immediately regardless of folding status. If misfolding or lack of calcium-binding is detected, limit applications to linear epitope antibody production and basic biophysical characterization, avoiding all functional interaction and comparative studies. For reliable oncomodulin research, always include appropriate calcium-binding controls and consider the protein's calcium-dependent conformational changes in experimental design.
