Recombinant Dog Erythropoietin receptor (EPOR) is expressed in E. coli with a partial sequence spanning amino acids 25 to 250. This protein features both N-terminal 6xHis-GB1 and C-terminal 6xHis tags, which aid in purification and detection. The purity level exceeds 85% as verified by SDS-PAGE, ensuring reliable experimental results. This product is designed for research use only and is not suitable for therapeutic or diagnostic applications.
The erythropoietin receptor (EPOR) appears to be a critical component in regulating erythropoiesis—the process of red blood cell production. It works by binding to erythropoietin, triggering a cascade of intracellular signaling pathways that promote cell survival, proliferation, and differentiation. EPOR plays a significant role in studies related to blood cell formation and may offer insight into conditions affecting red blood cell levels.
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. Protein-Protein Interaction Studies
This dual-tagged EPOR fragment can be used in pull-down assays to identify and characterize proteins that interact with the extracellular domain of canine erythropoietin receptor. The N-terminal His-GB1 tag provides enhanced solubility and proper folding. Meanwhile, the C-terminal His tag offers additional purification and immobilization options. The expressed region (25-250aa) likely encompasses key extracellular domains involved in ligand binding and protein interactions, though the exact functional boundaries remain to be confirmed. Such studies could help clarify the molecular mechanisms of erythropoietin signaling in canine models.
2. Antibody Development and Screening
The recombinant protein can serve as an immunogen or screening antigen for developing antibodies specific to canine EPOR. Both His tags make purification and immobilization on various surfaces straightforward for ELISA-based antibody screening assays. Given the high purity (>85%), this protein provides a reliable antigen source for both polyclonal and monoclonal antibody production targeting the extracellular domain of canine EPOR.
3. Comparative Species Analysis
This canine EPOR fragment may prove useful in comparative studies examining structural and functional differences between human and canine erythropoietin receptors. Researchers can use the protein in binding assays to compare cross-reactivity patterns with various erythropoietin ligands or receptor-binding proteins across species. These research applications could be valuable for understanding evolutionary conservation of EPOR function and for developing appropriate animal models, though species-specific differences might limit direct translational insights.
4. Structural and Biophysical Characterization
The GB1 domain fusion enhances protein stability and solubility, making this construct suitable for biophysical studies such as circular dichroism spectroscopy, dynamic light scattering, or NMR analysis. The dual tagging system allows for oriented immobilization in surface plasmon resonance experiments to study binding kinetics with potential ligands. These applications can provide insights into the structural properties of the canine EPOR extracellular domain, though the presence of tags may influence some measurements.
