Recombinant Human Interferon lambda-1 protein (IFNL1) is produced in E. coli and contains the complete mature protein sequence from amino acids 20-200. This tag-free protein achieves purity levels above 97% based on SDS-PAGE analysis. The protein shows full biological activity, with an ED50 below 5 ng/ml when tested in anti-viral assays using human HepG2 cells. Endotoxin levels remain under 1.0 EU/µg, which appears to make it well-suited for high-quality research work.
Interferon lambda-1 belongs to the type III interferon family and seems to play an important role in how the immune system responds to viral infections. What makes it particularly interesting is that it signals through a receptor complex that's different from type I and II interferons. This pathway primarily targets epithelial cells. Scientists are drawn to this protein because of its involvement in antiviral defense and its potential therapeutic uses - it may be able to modulate immune responses without causing the inflammatory side effects that often come with other interferons.
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. Antiviral Activity Screening and Mechanism Studies
This recombinant IFNL1 protein is confirmed to be biologically active (ED₅₀ < 5 ng/ml in HepG2 antiviral assays) and suitable for antiviral studies. However, researchers should validate its activity in other cell types expressing the interferon lambda receptor complex (IFNLR1/IL10RB), particularly primary human hepatocytes and epithelial cells, where IFNL1 signaling is most physiologically relevant. The high purity (>97%) supports reliable results, but optimal concentrations may need adjustment for different viral challenge models beyond encephalomyocarditis virus.
2. Interferon Lambda Receptor Binding and Signaling Studies
The biologically active IFNL1 is appropriate for IFNLR1/IL10RB binding and JAK-STAT signaling studies. The demonstrated activity in human HepG2 cells confirms proper folding for receptor engagement, but researchers should validate binding kinetics in receptor-specific systems. The tag-free design ensures authentic interactions, but signaling studies should focus on ISG expression profiling in addition to STAT phosphorylation to fully characterize pathway activation.
3. Comparative Interferon Response Analysis
This IFNL1 enables valid comparisons with type I interferons, but researchers should account for tissue-specific receptor distribution - IFNLR1 is predominantly expressed in epithelial cells rather than ubiquitously like type I interferon receptors. Comparative transcriptomic studies should use appropriate cell models (e.g., primary hepatocytes, airway epithelia) to capture physiologically relevant differences between interferon classes.
4. Antibody Development and Validation
This high-purity, full-length IFNL1 (20-200aa) serves as an excellent antigen for antibody development. However, antibodies should be validated for specificity against other interferon lambda family members (IFNL2/3), which share significant sequence homology. The confirmed bioactivity supports the development of neutralizing antibodies, but comprehensive validation should include testing in physiologically relevant epithelial cell systems.
5. Cell-Based Assay Development and Standardization
The protein is suitable for assay development, but the ED₅₀ was determined in a specific virus-cell system (HepG2/encephalomyocarditis virus) and may not directly translate to other assay formats. Researchers should establish system-specific dose-response curves when developing new reporter assays or screening platforms. The consistent activity supports standardization, but assay conditions may require optimization for different cellular contexts.
Final Recommendation & Action Plan
This recombinant human IFNL1 is a high-quality reagent with demonstrated antiviral activity, making it suitable for all proposed applications with appropriate validation for specific experimental systems. First, establish dose-response relationships in your target cell types, particularly focusing on epithelial cells and hepatocytes, which express the complete IFNLR1/IL10RB receptor complex. For antiviral studies, the <5 ng/ml ED₅₀ provides an excellent starting point, but validate against relevant viruses for your research questions. When developing antibodies, leverage the full-length protein for comprehensive epitope coverage but validate specificity against other interferon lambda family members. For signaling studies, the tag-free design ensures authentic receptor interactions but includes appropriate controls for tissue-specific responses. The E. coli expression produces a non-glycosylated protein, but as interferon lambdas are not heavily glycosylated, this should not significantly impact function. Always include proper interferon response controls (e.g., ISRE reporters, MX1 expression) and consider that different epithelial cell types may exhibit varying sensitivity to IFNL1 stimulation. The high purity and low endotoxin make this protein particularly valuable for sensitive primary cell assays where non-specific stimulation must be minimized.
