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.
1. Protein-Protein Interaction Studies Using Pull-Down Assays
The N-terminal 6xHis-tagged recombinant mouse Txndc12 can be attached to nickel-affinity resins to capture potential binding partners from mouse cell lysates or tissue extracts. This method may help reveal the molecular networks where Txndc12 operates in cellular processes. The high purity (>90%) should minimize background noise from contaminating proteins. Mass spectrometry analysis of captured complexes could uncover previously unknown interacting proteins and shed light on what Txndc12 actually does in cells.
2. Antibody Development and Validation
This recombinant protein works well as an immunogen for creating mouse Txndc12-specific antibodies in rabbits or other host animals. The mature protein region (25-170aa) represents what's found naturally, making it appropriate for producing antibodies that recognize the native form. The His-tag helps with protein purification during immunization procedures and later antibody testing through ELISA-based binding experiments. These antibodies could then be tested for use in Western blotting, immunoprecipitation, or immunofluorescence applications.
3. Biochemical Characterization and Structural Studies
The purified recombinant Txndc12 enables detailed biochemical analysis, including measuring protein stability, folding characteristics, and thermal breakdown patterns. Circular dichroism spectroscopy might reveal details about the secondary structure of this thioredoxin domain-containing protein. Researchers can test how the protein behaves under different buffer conditions, pH levels, and salt concentrations. These experiments would help determine the best conditions for storing and handling the protein in research settings.
4. Comparative Functional Analysis Across Species
This mouse Txndc12 protein can act as a reference point for comparing Txndc12 versions from other species. Testing cross-reactivity with antibodies developed against human or rat Txndc12 may show how well epitopes are conserved through evolution. The recombinant protein allows direct comparison of biochemical characteristics between different species variants. Such comparative work could reveal species-specific functional differences and evolutionary connections within the broader thioredoxin domain-containing protein family.
