Recombinant Human VEGF coregulated chemokine 1 protein (CXCL17) is produced in E. coli and represents the full length of the mature protein, spanning amino acids 22-119. This tag-free protein achieves a purity greater than 96% as confirmed by SDS-PAGE analysis. The protein demonstrates full biological activity, inducing VEGF expression with an ED50 of less than 5.0 μg/ml in murine endothelial cells, which corresponds to a specific activity greater than 200 IU/mg. Endotoxin levels remain controlled at less than 1.0 EU/μg, as measured by the LAL method.
CXCL17 appears to play an important role in immune cell recruitment and helps modulate inflammatory responses. The protein seems particularly relevant for angiogenesis regulation through its capacity to induce VEGF expression. This makes CXCL17 an intriguing target for vascular biology research, though our understanding of its complete functional network may still be developing. Researchers studying immune response and tissue repair mechanisms likely need to consider CXCL17's function and interactions.
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. VEGF Expression Induction Assays
This recombinant CXCL17 protein works well for studying VEGF expression regulation in endothelial cell models. Its demonstrated biological activity in murine endothelial cells (ED50 < 5.0 μg/ml) provides a reliable starting point for experiments. Scientists can examine dose-response relationships and track how VEGF induction changes over time. The downstream signaling pathways involved in angiogenic factor regulation also become accessible for investigation. High purity levels (>96%) and low endotoxin content make this protein particularly suitable for cell culture work where contaminants could skew results.
2. Chemokine Receptor Binding Studies
The biologically active CXCL17 protein serves as a ligand for receptor binding assays, helping identify and characterize its cognate receptors across different cell types. Competitive binding experiments, receptor internalization studies, and cross-linking assays may reveal important details about CXCL17-receptor interactions. Since this protein lacks fusion tags, binding studies should reflect native protein-receptor interactions more accurately, avoiding potential interference that tags sometimes introduce.
3. Angiogenesis Research Models
CXCL17's ability to induce VEGF expression opens doors for incorporating this protein into various in vitro angiogenesis assays. Endothelial cell migration, tube formation, and proliferation studies all become possible research directions. The defined specific activity (>200 IU/mg) helps establish standardized experimental conditions that different research groups can reproduce. Scientists can explore how CXCL17 influences angiogenic processes and investigate its potential interactions with other factors that either promote or inhibit angiogenesis.
4. Antibody Development and Validation
This high-purity, biologically active CXCL17 protein works as an excellent antigen for generating and validating antibodies against human CXCL17. Researchers can immunize animals, screen hybridomas, and test antibody specificity through ELISA, Western blotting, and neutralization assays. The confirmed biological activity offers a functional readout that's particularly valuable when testing whether antibodies can neutralize CXCL17's effects in VEGF induction assays.
5. Protein-Protein Interaction Studies
The recombinant CXCL17 proves useful in biochemical assays designed to identify and characterize protein-protein interactions. Potential binding partners, co-receptors, or regulatory proteins may emerge from such studies. Pull-down assays, surface plasmon resonance studies, or co-immunoprecipitation experiments can help map CXCL17's interaction network, though some interactions might be context-dependent or require additional cofactors. The mature protein region (22-119aa) represents the physiologically relevant form for these interaction studies.
