Recombinant Clostridium tetani Tetanus toxin (tetX) gets produced in E. coli and includes an N-terminal 6xHis-B2M tag that makes purification and detection more straightforward. This partial protein covers amino acids 2-457 and shows purity levels exceeding 85%, as confirmed through SDS-PAGE analysis. The product is designed strictly for research purposes and appears to provide a reliable source of tetanus toxin for different experimental work.
Clostridium tetani produces the naturally occurring tetanus toxin, which is recognized for its powerful neurotoxic properties that disrupt normal muscle contractions. It has become important in neurological research because of how it blocks neurotransmitter release at synapses, ultimately causing muscle paralysis. Getting a better grasp of its mechanism may be key for creating strategies to combat its effects and enhance therapeutic approaches.
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. Antibody Development and Characterization
This recombinant tetanus toxin fragment (amino acids 2-457) could work as an immunogen for creating monoclonal or polyclonal antibodies against tetanus toxin in research environments. The N-terminal 6xHis-B2M tag makes purification simpler and helps with immobilization for antibody screening assays. Scientists can incorporate this protein into ELISA-based assays to examine antibody binding specificity and affinity. The partial protein sequence likely represents particular domains of the toxin that matter for antibody recognition studies.
2. Protein-Protein Interaction Studies
The 6xHis-B2M tagged recombinant protein works well in pull-down assays to find and examine potential cellular binding partners or receptors that connect with tetanus toxin. The histidine tag allows for effective immobilization on nickel-based affinity matrices, which can capture interacting proteins from cell lysates or tissue extracts. This method may help scientists explore the molecular mechanisms behind tetanus toxin cellular interactions under controlled laboratory settings.
3. Biochemical and Structural Analysis
This purified recombinant protein fragment offers material for thorough biochemical characterization studies, including mass spectrometry, circular dichroism spectroscopy, and other analytical methods. The high purity (>85%) appears to make it appropriate for structural studies aimed at understanding the folding and stability characteristics of this particular tetanus toxin region. Scientists can conduct comparative analysis between different expression constructs or look into how various buffer conditions affect protein stability.
4. In Vitro Binding and Competition Assays
The recombinant tetanus toxin fragment can be used to create cell-free binding assays for studying toxin-receptor interactions or screening potential inhibitory compounds in research settings. The protein might serve as a competitor in displacement assays or function as a direct binding partner in surface plasmon resonance or other biophysical binding studies. These assays could generate quantitative data on binding kinetics and thermodynamics for basic research applications.
