Recombinant Mycobacterium paratuberculosis Probable transcriptional regulatory protein MAP_1030 is expressed in a yeast system as a full-length protein consisting of amino acids 1-250. The protein includes an N-terminal 6xHis-tag, which makes purification and detection straightforward. SDS-PAGE analysis shows it reaches a purity level greater than 85%, making it suitable for various research applications. This product is intended for research purposes only and is not for clinical use.
MAP_1030 appears to be a transcriptional regulatory protein from Mycobacterium paratuberculosis. It likely plays a role in gene regulation, though its exact function may involve influencing the transcription of specific genes within the bacterium. Research into the function and regulation of such proteins seems crucial for understanding bacterial gene expression and regulatory mechanisms. Studies of MAP_1030 might provide insights into the complex pathways and interactions within Mycobacterium species.
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
This recombinant transcriptional regulatory protein works well in pull-down assays to identify potential binding partners within Mycobacterium paratuberculosis or related mycobacterial species. The N-terminal 6xHis tag allows for immobilization on nickel-affinity matrices, capturing interacting proteins from bacterial lysates. Such studies could reveal regulatory networks and protein complexes involved in M. paratuberculosis gene expression. Using the full-length protein (1-250aa) helps ensure that all potential interaction domains remain intact for these binding studies.
2. DNA-Protein Interaction Analysis
Since MAP_1030 is probably a transcriptional regulatory protein, researchers can use it in electrophoretic mobility shift assays (EMSA) or surface plasmon resonance studies to investigate its DNA-binding properties. Scientists can test whether the protein binds to promoter regions or specific DNA sequences from the M. paratuberculosis genome. The yeast expression system may provide proper eukaryotic folding that could be necessary for DNA-binding activity. These studies would help clarify the regulatory targets and mechanisms of this transcriptional regulator.
3. Antibody Development and Validation
The purified recombinant protein works as an effective immunogen for generating polyclonal or monoclonal antibodies specific to MAP_1030. Both the high purity (>85%) and full-length nature of the protein help ensure comprehensive epitope representation for antibody production. Researchers could then use these antibodies for Western blotting, immunoprecipitation, or immunofluorescence studies in M. paratuberculosis research. The His-tag also allows the protein to serve as a positive control in various immunoassays during antibody characterization.
4. Structural and Biophysical Characterization
Researchers can use this recombinant protein in structural biology approaches such as X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to determine its three-dimensional structure. Biophysical techniques including dynamic light scattering, circular dichroism spectroscopy, and thermal stability assays may provide insights into the protein's folding, stability, and conformational properties. The yeast expression system might provide post-translational modifications that contribute to proper protein folding. Understanding the structure-function relationship of this transcriptional regulator would advance knowledge of mycobacterial gene regulation mechanisms.
5. Comparative Mycobacterial Studies
Scientists can use the recombinant MAP_1030 protein in comparative studies to investigate evolutionary relationships and functional conservation among mycobacterial transcriptional regulators. Cross-reactivity studies with related proteins from M. tuberculosis, M. avium, or other mycobacterial species could reveal conserved regulatory mechanisms. The protein can also serve as a reference standard in proteomic analyses comparing different mycobacterial strains or growth conditions. Such comparative approaches may identify species-specific regulatory features that distinguish M. paratuberculosis from other mycobacteria.
