Recombinant Rat Eotaxin protein (Ccl11) is produced using an E. coli expression system, achieving purity levels exceeding 96% as confirmed by SDS-PAGE analysis. This tag-free protein represents the complete mature protein sequence, spanning residues 24 to 97. The protein demonstrates biological activity and shows efficacy in chemotaxis bioassays with purified eosinophils within a concentration range of 0.1-1.0 μg/ml. Endotoxin levels remain below 1.0 EU/μg, as determined by the LAL method.
Eotaxin, also known as Ccl11, functions as a chemokine that appears critical for recruiting eosinophils—specialized white blood cells that participate in immune responses, particularly during allergic and asthmatic reactions. It likely plays a significant role in directing eosinophil migration to inflammatory sites, which makes it an important research target for studying immune system function and inflammatory diseases.
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. Eosinophil Chemotaxis Assays
This recombinant rat eotaxin protein works well as a positive control or standard in chemotaxis assays designed to study how eosinophils migrate. Its proven biological activity within the 0.1-1.0 μg/ml concentration range with purified eosinophils provides researchers with a dependable tool for investigating eosinophil recruitment mechanisms. Scientists can establish dose-response curves and validate experimental conditions in transwell migration assays using this protein. The high purity (>96%) and low endotoxin levels make it well-suited for sensitive cell-based functional studies.
2. Comparative Species Studies of Chemokine Function
The rat-specific sequence allows for comparative studies that examine species differences in chemokine-receptor interactions and signaling pathways. Researchers may compare this rat eotaxin's activity with human or mouse versions to understand how eosinophil recruitment mechanisms have been conserved through evolution. This application proves particularly valuable for translational research where rat models help study eosinophil-mediated processes. The tag-free design suggests that any observed differences likely reflect genuine species-specific variations rather than artifacts from protein tags.
3. Antibody Development and Validation
This highly pure recombinant protein serves as an excellent antigen for generating rat eotaxin-specific antibodies or validating existing antibody reagents. The complete mature protein sequence (24-97aa) offers the full antigenic profile needed for immunization protocols or ELISA-based detection systems. Scientists can establish standard curves for quantitative immunoassays or test antibody specificity and cross-reactivity using this protein. Low endotoxin content becomes particularly important during immunization procedures to minimize non-specific immune responses.
4. Receptor Binding and Competition Studies
The biologically active recombinant protein can be applied in receptor binding assays to investigate eotaxin-receptor interactions and identify potential competitive inhibitors. Scientists may use this protein in displacement studies to characterize binding affinities and kinetics with eosinophil surface receptors. The defined biological activity range (0.1-1.0 μg/ml) provides a useful reference point for designing binding experiments with appropriate protein concentrations. Such studies appear valuable for understanding the molecular basis of eosinophil activation and developing research tools that modulate these interactions.
5. In Vitro Eosinophil Activation Studies
This recombinant eotaxin can be applied to investigate eosinophil activation responses beyond chemotaxis—including degranulation, cytokine production, and changes in surface marker expression. The confirmed biological activity should ensure reliable eosinophil stimulation under controlled experimental conditions. Researchers can examine downstream signaling pathways activated by eotaxin treatment and study the timing of eosinophil responses. High purity and low endotoxin levels become critical for these applications to ensure that observed cellular responses stem specifically from eotaxin stimulation rather than contaminating factors.
