This recombinant Mouse Tenascin (Tnc) comes from a mammalian cell expression system and represents a partial protein spanning amino acids 1884-2099. The protein carries both an N-terminal 10xHis-tag and a C-terminal Myc-tag, which should make purification and detection more straightforward. SDS-PAGE analysis indicates the purity exceeds 85%, suggesting it's well-suited for laboratory work. This product is for research use only.
Tenascin appears to be a key extracellular matrix protein with important roles in how tissues develop and repair themselves. The protein seems to influence cell signaling pathways that control how cells stick together, move around, and differentiate into specialized types. Developmental biologists and cancer researchers pay particular attention to tenascin since its expression patterns often change dramatically in these contexts. Studying how this protein works and what it interacts with might reveal important details about these biological processes.
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 mouse Tenascin fragment (amino acids 1884-2099) could work well as an immunogen or coating antigen when developing antibodies that target this specific C-terminal region of Tnc. The His and Myc tags should make purification easier and help with detection during antibody screening. Researchers might find this protein useful in ELISA-based screens to test antibody specificity and check for unwanted cross-reactions. Since it's made in mammalian cells, the protein folding and post-translational modifications are likely to be correct—something that may be important for proper antibody recognition.
2. Protein-Protein Interaction Studies
The C-terminal region of Tenascin contains functional domains that might interact with other extracellular matrix proteins, cell surface receptors, or various signaling molecules. This fragment could prove valuable in pull-down experiments, where the His tag allows for immobilization on nickel resins to fish out potential binding partners from cell lysates or tissue samples. The Myc tag makes it simple to detect and confirm the bait protein during Western blot analysis. These kinds of studies may help researchers figure out exactly how Tenascin organizes the extracellular matrix at the molecular level.
3. Biochemical Characterization and Structural Studies
Having this purified Tenascin fragment opens up possibilities for detailed biochemical analysis of the C-terminal region's characteristics—things like how stable it is at different temperatures, how it responds to pH changes, and whether it forms oligomers. The high purity (>85%) suggests it should work well with biophysical methods like dynamic light scattering, circular dichroism spectroscopy, or analytical ultracentrifugation. Both tags give researchers multiple ways to detect and measure the protein during these experiments. Such work might reveal important structural features and stability patterns for this particular Tenascin domain.
4. Cell Adhesion and Migration Assays
Researchers could coat culture plates with this Tenascin fragment to create controlled extracellular matrix environments and watch how different mouse cell lines respond. This approach allows scientists to investigate whether the protein affects how cells attach, spread out, or migrate across surfaces. This specific amino acid region might contain cell-binding domains or sequences that actually discourage cell adhesion—both scenarios could influence how cells behave. In vitro experiments like these may help determine what role this particular piece of Tenascin plays in cell-matrix interactions.
5. Competitive Binding and Inhibition Studies
This fragment might serve as a competitor or inhibitor in experiments designed to study how full-length Tenascin interacts with cellular receptors or other matrix components. Running competition experiments with this recombinant piece could help researchers determine whether the C-terminal region (amino acids 1884-2099) is actually necessary for specific biological interactions. The tagged protein is easy to measure and track during these assays, which should allow for careful dose-response studies. Experiments like these may help map out which parts of the full-length Tenascin protein are functionally important and identify where critical binding sites are located.
