Recombinant Mouse Chordin-like protein 1 (Chrdl1) is produced through a baculovirus expression system, spanning the full length of the mature protein from amino acids 23 to 447. The protein includes an N-terminal 10xHis tag and a C-terminal Myc tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the protein achieves greater than 85% purity, though this may vary slightly between batches depending on expression conditions.
Chordin-like protein 1 (Chrdl1) appears to play an important role in controlling signaling pathways during embryonic development and tissue homeostasis. Current research suggests it interacts with and regulates various growth factors, which likely influences how cells differentiate and multiply. This makes Chrdl1 particularly interesting for developmental biology studies, though our understanding of its complete regulatory network remains incomplete.
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
This recombinant mouse Chrdl1 protein works well as an immunogen for creating polyclonal or monoclonal antibodies that specifically target Chrdl1. The dual-tagged design (N-terminal His and C-terminal Myc) offers several epitopes for antibody recognition and validation through Western blot, ELISA, or immunoprecipitation assays. While the >85% purity level should be adequate for most immunization protocols, some researchers might prefer additional purification steps for particularly sensitive applications. The resulting antibodies can help scientists track Chrdl1 expression and location in mouse tissues and cell lines, though cross-reactivity with related proteins may need to be assessed.
2. Protein-Protein Interaction Studies
The His and Myc tags make this protein well-suited for pull-down assays and co-immunoprecipitation experiments aimed at finding Chrdl1's binding partners. Researchers can immobilize the protein on nickel-based resins using the His-tag, then screen for binding partners with cell lysates or purified protein libraries. The Myc-tag offers an alternative route for immunoprecipitation studies with anti-Myc antibodies. However, it's worth noting that some interactions might be missed due to the artificial tags potentially interfering with native binding sites.
3. ELISA-Based Binding Assays
Scientists can develop sandwich or competitive ELISA assays using this recombinant protein to study how Chrdl1 interacts with other proteins or small molecules. The His-tag allows for oriented attachment to nickel-coated plates, while the Myc-tag can function as a detection point using anti-Myc antibodies. The >85% purity appears sufficient for establishing reliable ELISA protocols, though background signals from contaminant proteins might occasionally require troubleshooting. These assays could help researchers screen for potential binding partners or measure binding strengths under controlled laboratory conditions.
4. Biochemical Characterization Studies
This recombinant Chrdl1 protein serves as a good starting point for basic biochemical analyses, including molecular weight verification, thermal stability testing, and buffer optimization experiments. The baculovirus expression system generally produces properly folded proteins, which should make it compatible with biophysical techniques like dynamic light scattering or analytical ultracentrifugation. The dual-tag system helps with protein detection and measurement during these studies. Still, researchers should keep in mind that the tags might slightly alter the protein's natural behavior compared to the native form.
