Recombinant Arabidopsis thaliana 2-Cys peroxiredoxin BAS1, chloroplastic (BAS1) is produced in a yeast expression system, covering the mature protein from amino acids 66 to 266. The protein is expressed with an N-terminal 6xHis-tag to aid in purification and detection. Purity exceeds 90% as verified by SDS-PAGE, which appears to ensure reliable results for research applications.
2-Cys peroxiredoxin BAS1 plays a critical role in redox regulation within chloroplasts of Arabidopsis thaliana. It's involved in detoxifying peroxides and maintaining cellular redox homeostasis. This protein serves as a valuable tool for studying oxidative stress responses and redox signaling pathways in plants. It may provide insights into plant physiology and stress tolerance 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 His-Tag Pull-Down Assays
The N-terminal 6xHis-tag on this recombinant BAS1 protein allows for nickel-affinity based pull-down experiments to identify potential interaction partners from Arabidopsis chloroplast extracts. Being a chloroplastic 2-Cys peroxiredoxin, BAS1 likely participates in redox regulation networks within the chloroplast. This makes it valuable for mapping these protein interaction networks, though results will depend on experimental conditions. The >90% purity should minimize background binding from contaminant proteins during pull-down experiments. This approach could help clarify the molecular mechanisms of chloroplast redox homeostasis in plant cells.
2. Antibody Development and Validation
The high purity (>90%) and defined expression region (66-266aa) make this recombinant protein suitable as an immunogen for generating specific antibodies against Arabidopsis BAS1. The recombinant protein can serve as both positive control and standard for antibody specificity testing through Western blot, ELISA, and immunoprecipitation assays. Its His-tag makes purification and immobilization straightforward for antibody screening and validation experiments. These antibodies would likely become valuable research tools for studying BAS1 expression and localization in plant tissues.
3. Biochemical Characterization and Enzyme Kinetics Analysis
This recombinant BAS1 protein can be used for detailed biochemical characterization studies. These include thermal stability analysis, pH optimization, and cofactor requirements typical of 2-Cys peroxiredoxins. The high purity level allows for reliable spectrophotometric and fluorometric assays to determine basic biochemical properties, though some variation between batches may still occur. Researchers can investigate the protein's response to various reducing agents and oxidative conditions to understand its redox behavior. The defined expression region should ensure relatively consistent results across different experimental batches.
4. Comparative Structural and Functional Studies
The recombinant BAS1 protein enables comparative studies with other plant peroxiredoxins or homologous proteins from different species. This may help researchers understand evolutionary relationships and functional conservation within this protein family. The yeast expression system and high purity should make experiments reproducible when comparing enzymatic properties, stability, and molecular interactions. Researchers can use this protein alongside other recombinant peroxiredoxins to study structure-function relationships. The His-tag allows for standardized purification protocols across different protein variants, which is important for fair comparison.
