Recombinant Mouse Thioredoxin domain-containing protein 12 (Txndc12) is produced in E. coli and includes an N-terminal 6xHis-tag that makes purification more straightforward. The protein covers the complete mature protein sequence from amino acids 25 to 170. Purification achieves greater than 90% purity based on SDS-PAGE analysis, which appears to provide reliable quality for research work.
Thioredoxin domain-containing protein 12 (Txndc12) participates in redox homeostasis within cells. It seems to play an important role in keeping the cellular redox environment balanced, helping reduce disulfide bonds in proteins. Txndc12 belongs to the thioredoxin family, which is likely essential for antioxidant defense systems and cellular signaling networks. This makes it a compelling target for studying oxidative stress and related cellular mechanisms.
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.
Txndc12 is a thioredoxin domain-containing protein that typically requires proper disulfide bond formation and correct folding of its thioredoxin domain for functional activity. While E. coli can successfully express some redox-active proteins, the correct folding and functional activity cannot be guaranteed without validation. The thioredoxin domain requires specific structural features for its proposed redox regulatory functions. No validation data (e.g., redox activity assays, structural analysis) are provided. Therefore, the protein's folding status and bioactivity remain unverified, and applications should be considered conditional until functional validation is performed.
1. Protein-Protein Interaction Studies Using Pull-Down Assays
If the recombinant Txndc12 is correctly folded, the His-tag enables pull-down assays to identify potential binding partners from mouse cell lysates, as proper folding is essential for biologically relevant protein interactions. However, if misfolded, there is risk of non-specific binding or failure to recognize genuine biological partners, compromising the validity of identified interaction networks. The high purity helps reduce background, but cannot compensate for structural defects.
2. Antibody Development and Validation
This recombinant Txndc12 can be used as an immunogen for antibody generation regardless of folding status, as antibodies primarily recognize linear epitopes. The mature protein region provides appropriate epitope coverage for producing antibodies that recognize the native form. However, if misfolded, generated antibodies may not optimally recognize conformation-dependent epitopes of the properly folded protein in biological contexts.
3. Biochemical Characterization and Structural Studies
If properly folded, the recombinant protein is suitable for biochemical analysis and structural studies to understand Txndc12's properties, as these techniques rely on native conformation for meaningful insights. However, if misfolded, characterization data would misrepresent the native protein's structure and stability, leading to incorrect conclusions about its biochemical behavior.
4. Comparative Functional Analysis Across Species
If correctly folded and functional, mouse Txndc12 could serve as a reference for comparative studies with orthologs from other species, as valid comparisons require native protein structure and activity. However, if misfolded, any comparative data on epitope conservation or biochemical characteristics would be biologically irrelevant and misleading for understanding evolutionary relationships.
Final Recommendation & Action Plan
Before employing this recombinant Txndc12 in any application, it is essential to validate protein folding and bioactivity through functional assays (e.g., testing redox activity using appropriate substrates) and biophysical characterization (e.g., circular dichroism spectroscopy to confirm secondary structure, analysis of disulfide bond formation); if validation confirms proper folding and function, proceed with applications while including appropriate controls, but if the protein is misfolded or inactive, consider using alternative expression systems that better support proper folding of redox-active proteins or obtain a commercially validated standard to ensure reliable results in all proposed applications.
