Recombinant Rat Transforming growth factor beta-1 proprotein (Tgfb1) is expressed in E. coli with an N-terminal 6xHis-tag for easy purification. The protein includes the amino acids 30-278, representing a partial sequence of the full-length protein. This product achieves a purity greater than 85% as verified by SDS-PAGE, making it suitable for various laboratory applications. It is offered for research use only and not for diagnostic or therapeutic purposes.
Transforming growth factor beta-1 (TGF-beta1) appears to be one of the more crucial cytokines involved in regulating cell growth, differentiation, and immune responses. Part of the broader TGF-beta superfamily, it likely plays significant roles in cellular processes and participates in numerous signaling pathways. Scientists have extensively studied TGF-beta1 for its impact on fibrosis, wound healing, and immune system modulation, which may explain why it has become a key focus across various research areas.
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. Antibody Development and Validation Studies
This recombinant rat TGF-β1 proprotein can serve as an immunogen or antigen for developing antibodies specific to the rat TGF-β1 proprotein form. The N-terminal 6xHis tag makes purification and immobilization relatively straightforward for antibody screening assays. Researchers might find this protein useful in ELISA-based antibody characterization studies to determine binding specificity and affinity. The 85% purity level appears sufficient for most antibody development applications where complete homogeneity isn't necessarily critical.
2. Protein-Protein Interaction Studies
Pull-down assays become more manageable with the 6xHis tag, potentially helping identify binding partners of the TGF-β1 proprotein in rat cell lysates or tissue extracts. This approach could shed light on the molecular mechanisms involved in TGF-β1 proprotein processing and regulation. Scientists can immobilize the recombinant protein on nickel-affinity resins and use it to capture interacting proteins for subsequent mass spectrometry analysis. Such studies may reveal novel regulatory proteins involved in TGF-β1 signaling pathways, though results will likely require validation through additional methods.
3. Biochemical Characterization and Stability Studies
Investigating the biochemical properties of the TGF-β1 proprotein becomes possible with this recombinant version. This includes examining its stability under various pH and temperature conditions. Proteolytic cleavage studies might help researchers understand how the proprotein gets processed to release mature TGF-β1. The protein's behavior in different buffer systems and storage conditions can be systematically evaluated, though optimal conditions may vary between laboratory settings. These studies could provide fundamental insights into the proprotein's structural requirements for proper folding and processing.
4. Comparative Species Analysis
The rat-specific sequence makes this recombinant protein particularly valuable for comparative studies examining species differences in TGF-β1 proprotein structure and processing. Comparing the biochemical properties of this rat proprotein with human or mouse orthologs might reveal species-specific features that weren't previously obvious. Cross-reactivity studies with antibodies developed against human TGF-β1 could highlight both conserved and divergent epitopes. Such comparative analyses may contribute to understanding evolutionary relationships and species-specific regulatory mechanisms, though interpreting these differences in biological context remains challenging.
