Recombinant Mouse Thioredoxin domain-containing protein 12 (Txndc12) is produced using a yeast expression system. The protein represents the full length of the mature form, spanning amino acids 25 to 170. It comes with an N-terminal 6xHis tag, which appears to simplify both purification and detection processes. SDS-PAGE analysis suggests the product achieves greater than 90% purity, making it potentially useful for various experimental approaches.
Thioredoxin domain-containing protein 12 (Txndc12) seems to participate in cellular redox processes. It likely plays an important role in maintaining redox homeostasis within cells. The protein belongs to the thioredoxin family, which appears essential for reducing oxidative stress and may function as a key component in cellular signaling pathways. Understanding this protein could provide insights into redox biology and its role in both normal physiology and disease states.
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.
The recombinant mouse Txndc12 (25–170aa) expressed in yeast with an N-terminal 6×His tag represents the full-length mature protein, which substantially increases the likelihood of proper folding and native-like bioactivity. Txndc12 is a thioredoxin domain-containing protein localized in the endoplasmic reticulum, and its folding depends on the formation of correct disulfide bonds—a process yeast expression systems can usually support. Therefore, it is highly probable that this recombinant protein is folded correctly and retains partial or full enzymatic and binding activity characteristic of native Txndc12. However, experimental validation is still necessary to confirm functional integrity before using it for mechanistic or structural studies.
1. Protein-Protein Interaction Studies
This N-terminal 6×His-tagged Txndc12 can be used in pull-down or affinity assays to explore potential binding partners involved in endoplasmic reticulum protein folding or redox regulation pathways. The tag facilitates immobilization on nickel matrices, and the >90% purity supports reproducibility in interaction assays. If the protein is correctly folded, it can identify physiological binding partners through its functional thioredoxin domain. If misfolded, it can still serve for preliminary screening but may not reflect authentic interactions, since disulfide-dependent conformations are essential for Txndc12 function. Thus, folding validation should precede high-confidence interaction studies.
2. Antibody Development and Validation
The recombinant full-length mature Txndc12 (25–170aa) is well-suited for producing specific antibodies recognizing the native protein. Its high purity and defined domain coverage ensure epitope accessibility. If correctly folded, antibodies generated against this antigen are likely to recognize both native and denatured forms of Txndc12. If misfolded, it will still serve as an effective linear-epitope immunogen for Western blot or ELISA but may not yield antibodies that bind conformational epitopes in immunocytochemistry or immunoprecipitation. Thus, it is suitable for antibody generation but requires validation of native binding specificity.
3. Structural and Biochemical Characterization
This recombinant protein is a strong candidate for structural and biophysical studies, given it represents the full-length mature form and is likely properly folded in yeast. It can be used for CD spectroscopy, DLS, or redox potential measurements to assess structure and enzymatic behavior. If folding and homogeneity are confirmed, it could be extended to X-ray crystallography or NMR for detailed structural studies. If folding is uncertain, it should be used only for secondary structure or stability analysis, not for atomic-level structural determination.
4. ELISA-Based Quantitative Assays
The His-tagged Txndc12 can be effectively used as a standard or capture reagent in ELISA assays to quantify Txndc12 expression levels in mouse samples. The >90% purity supports accurate quantitation with minimal nonspecific binding. If folded correctly, it provides a biologically relevant standard for quantifying native Txndc12. If misfolded, it can still function as a reference antigen for antibody calibration in denatured or tag-based ELISA formats.
