Recombinant Helicobacter pylori DNA protection during starvation protein (dps) is produced in E.coli and contains the complete protein sequence from amino acids 1 to 144. The protein comes with an N-terminal 6xHis-SUMO tag that makes purification and detection more straightforward. SDS-PAGE analysis confirms the product reaches a purity level greater than 90%, which appears suitable for research applications.
The DNA protection during starvation protein (dps) in Helicobacter pylori seems to play a critical role in protecting DNA under oxidative stress and during periods of nutrient deprivation. It's involved in forming a compact nucleoid that may shield DNA from damage. This has made it a significant focus of research in bacterial survival mechanisms and stress responses.
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-SUMO tag allows for nickel affinity-based pull-down experiments to identify potential binding partners of H. pylori Dps protein. Researchers can immobilize the recombinant protein on nickel-coated beads and incubate it with bacterial lysates or purified proteins to capture interacting molecules. The >90% purity should minimize background binding from contaminants. This approach might reveal novel regulatory networks involving Dps in H. pylori stress response pathways.
2. Antibody Development and Validation
The high purity recombinant Dps protein could serve as an excellent immunogen for generating polyclonal or monoclonal antibodies specific to H. pylori Dps. Since the full-length protein (1-144aa) contains all native epitopes, it should provide comprehensive antibody recognition. Researchers can validate generated antibodies using Western blot, immunoprecipitation, or ELISA formats with the same recombinant protein as a positive control. These antibodies would likely prove valuable for studying Dps expression and localization in H. pylori research.
3. Biochemical Characterization and Protein Stability Studies
The purified recombinant protein makes detailed biochemical analysis possible, including thermal stability, pH tolerance, and oligomerization studies. Techniques such as dynamic light scattering, differential scanning calorimetry, and analytical ultracentrifugation can be applied. SUMO protease treatment can remove the SUMO tag to study the native protein properties. These studies would provide fundamental insights into Dps protein behavior under various environmental conditions relevant to H. pylori survival strategies.
4. Comparative Proteomics and Cross-Species Analysis
The recombinant H. pylori Dps protein can serve as a reference standard in comparative studies with Dps homologs from other bacterial species. The high purity allows for accurate quantitative comparisons using mass spectrometry-based approaches. The His-tagged protein makes consistent purification protocols possible for parallel studies. Such comparative analyses might reveal species-specific adaptations and evolutionary relationships within the Dps protein family.
