Recombinant Dahlia merckii Defensin-like protein 1 is produced in E. coli and features an N-terminal 6xHis-B2M tag for easier purification and detection. The protein appears to be expressed as a full-length peptide covering amino acids 1 to 50, achieving what seems to be a purity level exceeding 90%, as verified by SDS-PAGE analysis. This product is intended for research use only.
Defensin-like proteins are small, cysteine-rich peptides that likely play a role in the innate immune response of plants. They may participate in various defense mechanisms by disrupting pathogen cell membranes. These proteins could prove valuable in research focused on plant immunity, offering insights into pathogen resistance and potential applications in agriculture.
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. Plant Defensin Structure-Function Analysis
This recombinant Dahlia merckii defensin-like protein might be used to investigate the structural characteristics and folding patterns typical of plant defensins through circular dichroism spectroscopy and NMR analysis. The N-terminal 6xHis-B2M tag should make protein purification and immobilization for biophysical studies more straightforward. Comparative structural analysis with other characterized plant defensins may help identify conserved motifs and unique features specific to dahlia species. The 50-amino acid length represents what appears to be a typical defensin domain size, making it suitable for detailed structural characterization studies.
2. Antimicrobial Activity Screening Assays
The protein could serve as a candidate for in vitro antimicrobial screening against various plant pathogens including fungi, bacteria, and potentially other microorganisms. Standard disk diffusion assays, minimum inhibitory concentration (MIC) determinations, and growth curve analyses can be performed to evaluate potential antimicrobial properties. The high purity (>90%) should ensure reliable and reproducible results in dose-response studies. These screening assays might contribute to understanding the defensive mechanisms that Dahlia merckii appears to use against pathogenic threats.
3. Antibody Development and Immunological Studies
The recombinant protein could be used as an immunogen for generating polyclonal or monoclonal antibodies specific to Dahlia merckii defensin-like proteins. The N-terminal tag system allows for easy purification and conjugation to carrier proteins for immunization protocols. These antibodies can subsequently be used for immunolocalization studies in dahlia tissues, protein expression analysis, and development of detection assays. The defined expression region (1-50aa) provides what may be a specific antigenic target for antibody production.
4. Protein-Protein Interaction Studies
The His-tagged protein might be used in pull-down assays to identify potential binding partners or target molecules that interact with dahlia defensin-like proteins. Immobilization of the protein on nickel-affinity matrices enables systematic screening of plant protein extracts or synthetic compound libraries. Co-immunoprecipitation experiments and surface plasmon resonance studies can further characterize binding kinetics and specificity. These interaction studies may reveal novel molecular mechanisms underlying defensin function in dahlia plants.
5. Comparative Plant Defense Protein Analysis
This recombinant protein could serve as a reference standard for comparative studies examining defensin-like proteins across different plant species and families. Phylogenetic analysis, sequence alignment studies, and cross-reactivity assays can be performed using this well-characterized protein as a benchmark. The standardized expression system and purification approach allow for consistent protein preparation across multiple research laboratories. Such comparative studies may contribute to understanding the evolution and diversification of plant defense mechanisms.
