Recombinant Mouse Interferon regulatory factor 8 (Irf8) is produced in E. coli and includes the complete protein sequence from amino acids 1 to 424. The protein carries an N-terminal 6xHis-SUMO tag that appears to improve both solubility and purification efficiency, reaching purity levels above 90% when verified through SDS-PAGE analysis. This high-quality recombinant protein is intended strictly for research purposes and may support a range of experimental applications.
Interferon regulatory factor 8 (Irf8) seems to play a central role in immune responses, particularly in controlling genes linked to immune cell differentiation and function. This transcription factor is likely crucial for modulating pathways in hematopoietic cells. Its influence on macrophage and dendritic cell development and function makes Irf8 activity essential for understanding immune regulation, with potentially significant implications for immunological research.
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. Protein-Protein Interaction Studies Using Pull-Down Assays
The N-terminal 6xHis-SUMO tag allows researchers to immobilize recombinant mouse Irf8 on nickel-based affinity resins during pull-down experiments. This method may help identify new protein partners that interact with Irf8 in mouse cell lysates or purified protein libraries. Since the full-length protein (1-424aa) retains all potential interaction domains, it appears well-suited for thorough binding studies. The >90% purity should minimize background interference from contaminating proteins during interaction screening.
2. Antibody Development and Validation
The recombinant full-length mouse Irf8 protein works well as an immunogen for creating mouse Irf8-specific antibodies in different species. High purity (>90%) and the complete protein length suggest that resulting antibodies will recognize native epitopes found in endogenous mouse Irf8. Researchers can also use the purified protein as a positive control in Western blotting, ELISA, and other immunoassays to confirm antibody specificity and find optimal working concentrations.
3. Biochemical Characterization and Stability Studies
The purified recombinant protein makes detailed biochemical analysis possible, including thermal stability profiling, pH tolerance testing, and buffer optimization studies. Such experiments may reveal optimal storage conditions and handling protocols for mouse Irf8. However, the E. coli expression system and SUMO tag could affect protein folding, which makes comparative studies with native protein particularly important for understanding any structural differences.
4. Tag-Based Purification Method Development
The 6xHis-SUMO tag system offers a chance to refine and standardize purification protocols for Irf8 family proteins. Researchers might test different elution conditions, buffer systems, and tag removal strategies using SUMO proteases. This protein could serve as a useful model for developing scalable purification workflows that may be applied to other interferon regulatory factor family members or related transcription factors.
