Recombinant Rat Oncostatin-M (Osm) gets expressed in E. coli and includes the complete mature protein sequence, covering amino acids 26 to 208. The product comes with an N-terminal 10xHis-tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the purity reaches above 85%, suggesting it should work reliably in research settings. Keep in mind this recombinant protein is strictly for research purposes—it's not appropriate for clinical or diagnostic use.
Oncostatin-M (Osm) belongs to the interleukin-6 cytokine family. This protein appears to play a significant role in controlling inflammation and how cells differentiate. Researchers often examine Osm because of its involvement in cell signaling pathways, especially those that influence immune responses and hematopoiesis. Its regulatory functions have made it a key target in studies looking at cellular growth and development.
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 Studies
This recombinant rat Oncostatin-M protein works well as an immunogen for creating polyclonal or monoclonal antibodies that target rat OSM specifically. The N-terminal 10xHis tag makes purification simple and allows for easy immobilization during antibody screening assays. Since purity exceeds 85%, the protein quality appears sufficient for immunization protocols and follow-up antibody characterization work. Because it contains the full-length mature protein sequence, any antibodies developed should recognize native epitopes found in endogenous rat OSM.
2. Protein-Protein Interaction Studies
Researchers can use this His-tagged recombinant protein in pull-down assays to find and characterize OSM binding partners within rat cell lysates or tissue extracts. The 10xHis tag allows for immobilization on nickel-affinity matrices, making it possible to systematically screen for proteins that might interact with OSM. Such studies may help clarify OSM signaling pathways and receptor interactions in rat models. The purified protein also serves as a useful control in competitive binding experiments when validating specific interactions.
3. ELISA Development and Optimization
The recombinant rat OSM protein can function as either a standard or coating antigen when developing enzyme-linked immunosorbent assays to detect OSM in rat biological samples. Its His tag allows for oriented immobilization on nickel-coated plates, which could improve both assay sensitivity and reproducibility. Given its defined concentration and purity level, the protein offers a dependable reference standard for quantitative measurements. This application supports preclinical research that requires OSM quantification in rat serum, plasma, or tissue homogenates.
4. Biochemical Characterization and Stability Studies
The purified recombinant protein proves useful for investigating rat OSM's biochemical properties, including thermal stability, pH sensitivity, and optimal storage conditions. SDS-PAGE analysis can verify protein integrity under different experimental conditions. The protein may serve as a substrate for studying post-translational modifications or proteolytic processing that's relevant to OSM biology. These characterization studies provide essential baseline data for designing functional experiments and understanding how OSM protein behaves in laboratory conditions.
