Recombinant Mouse C-X-C motif chemokine 9 protein (Cxcl9) is produced in E. coli and covers amino acid sequence 22-126 of the protein. This tag-free product achieves purity greater than 95% as determined by SDS-PAGE, with endotoxin levels below 1.0 EU/µg, verified by the LAL method. The protein appears to be fully biologically active, demonstrated by its ability to induce chemotaxis of human lymphocytes at concentrations ranging from 0.1 to 1.0 ng/ml.
Also known as MIG (monokine induced by gamma interferon), Cxcl9 is a chemokine that participates in immunological responses, particularly lymphocyte recruitment. The protein plays a significant role in inflammation and immune surveillance by guiding immune cells to sites of infection or injury. Because of its important role in immune signaling pathways, Cxcl9 represents a crucial protein for research into immune responses and inflammatory processes.
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. Lymphocyte Chemotaxis Assays
This recombinant mouse Cxcl9 protein is confirmed to be highly biologically active in human lymphocyte chemotaxis assays (active at 0.1-1.0 ng/ml) and suitable as a positive control. However, researchers should validate its activity in mouse-specific lymphocyte populations to confirm that cross-species reactivity is consistent. The exceptional potency (sub-nanogram range) and high purity support reliable dose-response studies, but optimal concentrations may need adjustment for primary mouse lymphocytes.
2. Comparative Species Cross-Reactivity Studies
The demonstrated human lymphocyte activity makes this protein valuable for cross-species studies, but researchers should confirm CXCR3 receptor binding specificity in both human and mouse systems. While the high potency suggests evolutionary conservation, quantitative comparisons should include parallel assays with both mouse and human Cxcl9 proteins to properly interpret species-specific differences in receptor affinity and signaling.
3. Antibody Development and Validation
This protein serves as a good antigen for antibody development, but the partial sequence (22-126aa) may not contain full epitopes present in the full-length protein. Antibodies should be validated against native mouse Cxcl9 from biological sources to ensure comprehensive epitope recognition. The high potency indicates proper folding of functional domains, supporting the generation of conformation-specific antibodies.
4. Protein-Protein Interaction Studies
The biologically active Cxcl9 is suitable for CXCR3 interaction studies, but the partial sequence may affect interactions with some co-receptors or glycosaminoglycans. Binding studies should focus on core CXCR3 interactions and validate any novel partners with full-length protein. The low endotoxin level ensures minimal interference in sensitive binding assays.
5. Structure-Function Relationship Analysis
This protein provides a good reference for structure-function studies, but the partial sequence limits analysis to the expressed region (22-126aa). Researchers studying regions outside this fragment should use full-length Cxcl9. The high potency confirms critical functional domains are present and properly folded in this truncated form.
Final Recommendation & Action Plan
This recombinant mouse Cxcl9 partial protein exhibits exceptional potency in human lymphocyte chemotaxis assays, making it suitable for most proposed applications. However, given its partial sequence (22-126aa) and demonstrated cross-species activity, researchers should: 1) First validate its activity in mouse-specific systems to confirm physiological relevance; 2) For antibody development, ensure generated antibodies recognize full-length native Cxcl9; 3) For interaction studies, focus on CXCR3 binding and validate novel interactions with full-length protein; 4) Leverage the high potency for sensitive chemotaxis assays but confirm optimal dosing in each specific experimental system. The E. coli expression produces a non-glycosylated protein, which may affect some interactions but appears sufficient for core receptor binding, given the demonstrated bioactivity. Always include appropriate species-matched controls when making cross-species comparisons.
