Recombinant Rat Oncostatin-M (Osm) is produced using a yeast expression system, which appears to ensure high yields of the full-length mature protein covering amino acids 26-208. The protein comes with an N-terminal 6xHis tag, making purification and detection more straightforward. SDS-PAGE analysis confirms the product displays a purity greater than 85%, though this level seems suitable for various research applications. It's provided as a research-use-only product with no detectable endotoxin levels.
Oncostatin-M (Osm) is a cytokine that likely plays a significant role in regulating inflammation, cell growth, and development across different biological systems. The protein appears to be involved in various signaling pathways, including those that may be critical for immune response modulation and tissue remodeling. Its importance in research stems from its involvement in these complex biological processes, making it a potentially valuable protein for studies in cellular signaling and cytokine interactions.
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. Antibody Development and Validation
This recombinant rat Oncostatin-M can serve as an immunogen for generating polyclonal or monoclonal antibodies specific to rat OSM. The N-terminal 6xHis tag makes purification and immobilization easier for antibody screening assays. Researchers can also use the protein as a positive control in Western blotting, ELISA, and immunohistochemistry experiments to validate antibody specificity. With greater than 85% purity, the protein quality appears sufficient for immunization protocols and subsequent antibody characterization studies.
2. Protein-Protein Interaction Studies
The 6xHis-tagged rat OSM works well in pull-down assays to identify potential binding partners or receptor interactions in rat cell lysates or tissue extracts. The His-tag makes immobilization on nickel-affinity matrices more straightforward, allowing for the capture and identification of interacting proteins through mass spectrometry analysis. This approach may help elucidate OSM signaling pathways and identify novel regulatory mechanisms in rat models. The mature protein region (26-208aa) represents the biologically relevant domain for such interaction studies.
3. Comparative Species Analysis
Researchers can use this rat OSM protein in comparative studies alongside human or mouse OSM orthologs to investigate species-specific differences in protein structure and binding properties. Cross-reactivity assays help determine whether antibodies or binding partners show species selectivity. Such comparative analyses prove valuable for translational research where findings from rat models need to be interpreted in the context of human biology. The yeast expression system provides a eukaryotic folding environment that likely preserves species-specific structural features.
4. Biochemical Characterization and Stability Studies
Scientists can use the recombinant protein for detailed biochemical analysis including thermal stability, pH sensitivity, and storage condition optimization studies. Analytical techniques such as dynamic light scattering, circular dichroism spectroscopy, and size exclusion chromatography may provide insights into protein folding, aggregation behavior, and structural integrity. These studies appear essential for establishing proper handling protocols and understanding the biophysical properties of rat OSM in research applications.
