Recombinant Mouse C-X-C motif chemokine 2 protein (Cxcl2) is produced in E. coli and covers the full length of the mature protein from amino acids 28-100. This tag-free protein achieves a purity level of over 97% as determined by SDS-PAGE. The protein appears to maintain full biological activity, as established through a chemotaxis bioassay using human neutrophils, with effective concentrations ranging from 1.0-10 ng/ml. Endotoxin levels remain below 1.0 EU/µg, verified by the LAL method.
C-X-C motif chemokine 2 (Cxcl2) is a chemokine that likely plays a key role in neutrophil chemotaxis and immune response. As part of the CXC chemokine family, it may be crucial for recruiting immune cells to inflammation or injury sites. Researchers often examine Cxcl2 for its role in inflammatory processes and its potential relevance across various fields, including immunology and cell signaling pathways.
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. Neutrophil Chemotaxis Assays
This recombinant mouse Cxcl2 protein works well as a positive control or test reagent in neutrophil migration studies using transwell or microfluidic chemotaxis chambers. Since it shows biological activity in human neutrophil chemotaxis assays at 1.0-10 ng/ml concentrations, researchers can establish dose-response curves and compare chemotactic responses across different experimental conditions. The high purity (>97%) and low endotoxin levels suggest it's suitable for primary cell-based assays where contamination might interfere with results. This approach proves particularly valuable for studying neutrophil recruitment mechanisms and inflammatory responses under controlled laboratory conditions.
2. Inflammatory Response Modeling in Cell Culture
The biologically active Cxcl2 protein can act as an inflammatory stimulus in various cell culture models to study chemokine signaling pathways and cellular responses. Researchers might use this protein to activate chemokine receptors on target cells and investigate downstream signaling cascades, gene expression changes, or protein modifications. The defined concentration range of biological activity (1.0-10 ng/ml) offers a starting point for dose optimization in different cell types. This application appears to support mechanistic studies of inflammation and immune cell activation in vitro.
3. Antibody Development and Validation
This recombinant Cxcl2 protein serves as an antigen for developing and characterizing anti-Cxcl2 antibodies for research applications. Its high purity and tag-free nature make it suitable for immunization protocols, ELISA development, and antibody specificity testing. Researchers can use this protein to validate antibody performance in various assays including Western blotting, immunoprecipitation, and flow cytometry applications. Having biologically active protein also enables functional antibody screening to identify neutralizing or non-neutralizing antibodies.
4. Protein-Protein Interaction Studies
The recombinant Cxcl2 protein works in biochemical assays to study its interactions with chemokine receptors or other binding partners. Surface plasmon resonance, bio-layer interferometry, or other label-free binding assays can use this protein to determine binding kinetics and affinities. The high purity and biological activity suggest that interaction studies may reflect physiologically relevant binding events. This application supports research into chemokine receptor pharmacology and the molecular basis of chemokine signaling.
5. Comparative Species Studies
This mouse Cxcl2 protein enables comparative studies with human or other species' chemokine orthologs to understand evolutionary conservation and species-specific differences in chemokine function. Researchers can compare the biological activity, receptor binding profiles, and functional responses between mouse and human systems using this well-characterized protein. The demonstrated cross-species activity with human neutrophils provides a foundation for such comparative analyses. This application appears valuable for translational research and understanding species differences in inflammatory responses.
