This recombinant Chlamydia trachomatis Major outer membrane porin (ompA), serovar A, is expressed in E. coli and contains the full length of the mature protein (23-396aa). It comes with an N-terminal 6xHis-SUMO tag that helps with purification and detection. SDS-PAGE analysis confirms the product shows purity levels above 90%, which appears to provide reliable performance for research applications.
The Major outer membrane porin of Chlamydia trachomatis, often called ompA, seems to play an important role in bacterial outer membrane structure. This protein is involved in maintaining membrane integrity and permeability, and it also functions in immune responses during infection. Given its significance in cellular interactions and potential as a vaccine target, ompA has become a key focus in microbial pathogenesis research.
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 Studies
This recombinant ompA protein can work as an immunogen for creating monoclonal or polyclonal antibodies specific to Chlamydia trachomatis serovar A. The N-terminal His-SUMO tag makes purification and immobilization easier for antibody screening assays. Scientists can apply this protein in ELISA-based assays to study antibody specificity, affinity, and cross-reactivity with other chlamydial serovars. The high purity (>90%) should help deliver consistent and reproducible results in immunological assays.
2. Protein-Protein Interaction Studies
The His-SUMO tagged ompA works well in pull-down assays to find host cell proteins that interact with the major outer membrane porin. The His tag allows immobilization on nickel-affinity matrices, while the SUMO tag offers additional purification options and may help stabilize the protein. This method can help researchers understand molecular mechanisms of chlamydial pathogenesis and host-pathogen interactions in controlled laboratory systems.
3. Structural and Biochemical Characterization
This recombinant protein offers a useful tool for studying the structural properties and biochemical features of Chlamydia trachomatis ompA. Researchers can apply techniques like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation. Since the mature protein region (23-396aa) is expressed in E. coli, it allows for isotopic labeling studies and NMR analysis. Scientists can examine protein folding, stability, and conformational changes under different buffer conditions and temperatures.
4. Vaccine Research and Immunogenicity Studies
The recombinant ompA protein can be used in preclinical vaccine development studies to measure immune responses in animal models. Researchers might evaluate the immunogenicity of various adjuvant formulations and delivery methods using this purified antigen. The protein serves as a standardized antigen for comparing immune responses across different experimental conditions and for fine-tuning vaccine formulations in laboratory settings.
5. Serovar-Specific Research Applications
This serovar A-specific ompA protein makes comparative studies possible with ompA proteins from other Chlamydia trachomatis serovars. Researchers can identify sequence and structural differences that may contribute to serovar specificity. Scientists can use this protein in competitive binding assays and cross-reactivity studies to better understand antigenic variation among different chlamydial strains. The standardized recombinant format should allow for consistent comparative analyses across multiple research laboratories.
