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.
Human OSM is a cytokine that requires precise folding, proper disulfide bond formation (with three conserved disulfide bonds), and specific tertiary structure for its functional activity in receptor binding and signaling. The E. coli expression system cannot provide the eukaryotic folding environment or oxidative conditions for correct disulfide bond formation. The partial fragment (26-221aa) lacks the complete structural context, and the large N-terminal 6xHis-SUMO tag (∼15 kDa) may sterically interfere with the protein's receptor-binding domains. While OSM can sometimes be refolded to activity, the probability of correct folding with functional receptor-binding activity requires experimental validation.
1. Antibody Development and Validation Studies
This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional protein folding. The partial protein provides specific epitopes within the 26-221aa region for generating antibodies against OSM. The high purity (>90%) ensures minimal contamination-related issues during immunization protocols.
2. Protein-Protein Interaction Studies
This application carries a significant risk without proper folding validation. OSM interactions with OSMR and gp130 receptors require precise tertiary structure and proper disulfide bonding. If misfolded/unverified, there is a high risk of non-specific binding or failure to replicate genuine receptor interactions. The large SUMO tag may sterically block receptor-binding interfaces.
3. Biochemical Characterization
These studies are essential for determining folding status. Techniques should include circular dichroism spectroscopy to assess secondary structure, size-exclusion chromatography to evaluate oligomeric state, and disulfide bond analysis. However, the SUMO tag may dominate the protein's biophysical properties and interfere with meaningful structural analysis.
4. Cell Culture Research Applications
This application carries a high risk without functional validation. OSM's biological activity in cell culture requires native conformation and proper receptor binding. If incorrectly folded, the protein will not elicit proper cellular responses and may yield biologically misleading results. The prokaryotic expression system lacks glycosylation, which may affect stability and activity.
Final Recommendation & Action Plan
The E. coli-expressed OSM fragment with a large SUMO tag poses significant challenges for functional applications due to the essential requirements for disulfide bond formation that cannot be guaranteed in this expression system. Begin with Application 3 (Biochemical Characterization) to assess folding quality through CD spectroscopy, SEC, and validate receptor-binding capability using known OSM receptors. Applications 2 and 4 require rigorous functional validation before proceeding. Application 1 (antibody development) can proceed immediately. For reliable OSM research requiring native functionality, use mammalian-expressed, properly folded protein that preserves conformational epitopes and receptor-binding capability.
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