Recombinant Human Oncostatin-M (OSM) is expressed in E.coli and includes the full length of the mature protein, covering the 26-221 amino acid region. The protein comes with an N-terminal 6xHis-SUMO tag that helps with purification, reaching over 90% purity when checked by SDS-PAGE. This product appears to be intended for research use only, though it seems to deliver consistent quality and performance across different experimental setups.
Oncostatin-M (OSM) is a cytokine that belongs to the interleukin-6 family. It's known for playing a role in inflammation and immune responses, though its exact mechanisms can be complex. OSM appears to be involved in several biological processes - cell proliferation, differentiation, and apoptosis among them. Researchers often examine how it affects signaling pathways like JAK-STAT and MAPK, which may be important for understanding how cells communicate and regulate immune functions.
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 human OSM protein might work well as an immunogen for creating monoclonal or polyclonal antibodies against human oncostatin-M. The high purity (>90%) and full-length mature protein structure suggest it could be suitable for immunization protocols in research animals. The N-terminal His-SUMO tag can be used for protein purification and immobilization in ELISA-based antibody screening assays. Researchers may find this protein useful for validating antibody specificity and cross-reactivity in Western blot, immunoprecipitation, and similar immunoassay applications.
2. Protein-Protein Interaction Studies
The His-SUMO tagged OSM protein could work in pull-down assays to identify and characterize potential binding partners or receptor interactions. The His tag allows for efficient immobilization on nickel-based affinity matrices, which can capture interacting proteins from cell lysates or purified protein preparations. This approach might help researchers study OSM's molecular interactions and binding kinetics in controlled in vitro environments. The SUMO tag offers additional purification options and may help maintain proper protein folding during expression and purification - though this isn't always guaranteed.
3. Biochemical Characterization and Structural Studies
This recombinant OSM protein appears to be a valuable tool for detailed biochemical analysis, including protein stability studies, folding kinetics, and biophysical characterization. The high purity level makes it potentially suitable for techniques such as circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation to assess protein structure and oligomerization states. Researchers can investigate the protein's thermal stability, pH sensitivity, and conformational changes under various buffer conditions - though results may vary depending on specific experimental conditions. The defined expression region (26-221aa) provides a consistent protein preparation for reproducible structural studies.
4. Cell Culture Research Applications
The recombinant OSM protein can serve as a research reagent in cell culture experiments to study cellular responses and signaling pathways. Researchers might add this protein to cell culture media to investigate its effects on cell proliferation, differentiation, or gene expression patterns in various human cell lines. The protein could serve as a positive control in cytokine signaling studies or as a tool to activate specific cellular pathways for mechanistic research. The E. coli expression system provides a cost-effective source of protein for dose-response studies and time-course experiments, though some researchers may prefer mammalian expression systems for certain applications.
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