Recombinant Mouse Interleukin-33 (Il33) is produced in an E.coli system, representing a partial protein sequence from amino acids 109 to 266. This tag-free protein exhibits a high purity level of over 95%, as confirmed by SDS-PAGE analysis. It demonstrates biological activity, verified through functional ELISA, showing specific binding to Mouse ST2-Fc with an ED50 of 0.33 µg/ml. The endotoxin level is controlled, measuring less than 1.0 EU/µg according to the LAL method.
Interleukin-33 (IL-33) is a cytokine involved in immune system signaling. It acts as an alarmin—basically a molecular distress signal released when cells are damaged. This protein appears to play a critical role in inflammatory and immune responses. IL-33 binds to the receptor ST2, which then activates pathways that influence how immune cells function. Its significance in research is underscored by its involvement in various immune-related processes, potentially offering insights into inflammation mechanisms and therapeutic targets.
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. IL-33/ST2 Receptor Binding Studies
This recombinant mouse IL-33 protein can be used to investigate how IL-33 and its receptor ST2 interact in laboratory settings. The confirmed biological activity, demonstrated through ST2-Fc binding with an ED50 of 0.33 μg/ml, provides a solid foundation for dose-response studies. Researchers might apply this protein in surface plasmon resonance (SPR) or bio-layer interferometry (BLI) experiments to determine detailed binding parameters. These studies appear essential for understanding the molecular mechanisms of IL-33 signaling pathways in mouse models.
2. Functional ELISA Development and Optimization
The protein's demonstrated binding capability in functional ELISA makes it suitable for developing standardized IL-33 detection assays. Researchers can use this recombinant protein as a positive control or standard when studying IL-33 levels in mouse tissue samples or cell culture supernatants. The high purity (>95%) and low endotoxin levels likely ensure reliable and reproducible results in quantitative assays. This application may be particularly valuable for preclinical studies investigating inflammatory responses or tissue damage models.
3. Anti-IL-33 Antibody Development and Validation
This biologically active recombinant mouse IL-33 can serve as an immunogen or screening antigen for generating and validating anti-IL-33 antibodies. The protein's confirmed receptor binding activity suggests that generated antibodies will recognize the functionally relevant form of IL-33. Scientists can use this protein in immunization protocols, antibody screening assays, and specificity testing. The tag-free nature of the protein eliminates potential cross-reactivity issues with purification tags during antibody development.
4. Cell-Based Functional Assays
The biologically active IL-33 protein can be applied in cell culture experiments to study IL-33-mediated cellular responses in mouse cell lines expressing ST2 receptors. Researchers might investigate downstream signaling pathways, cytokine production, or cellular activation using this protein as a stimulus. The low endotoxin level (<1.0 EU/μg) makes it suitable for sensitive cell-based assays where bacterial contamination could interfere with results. Such studies are crucial for understanding IL-33 biology in controlled laboratory environments.
5. Competitive Binding and Inhibition Studies
This recombinant IL-33 can be applied in competitive binding assays to screen for potential IL-33 antagonists or to study how mutations affect receptor binding. The established ED50 value provides a reference point for comparing the binding efficiency of modified IL-33 variants or testing whether small molecules can inhibit binding. Researchers can design competition experiments where this protein serves as the reference ligand against which other compounds are tested for their ability to disrupt IL-33/ST2 interactions.
