This recombinant Chlamydia trachomatis Major outer membrane porin, serovar B (ompA) comes from an E. coli expression system and contains the full length of the mature protein (23-394aa). The protein carries both an N-terminal 10xHis-tag and C-terminal Myc-tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows purity levels exceeding 85%, suggesting it should work well for different research applications.
The major outer membrane porin (ompA) of Chlamydia trachomatis appears to be essential for maintaining the bacterial outer membrane's structural integrity and controlling what passes through it. This component likely helps keep the membrane stable while managing the transport of small molecules. Researchers studying bacterial pathogenesis and looking for new therapeutic targets may find understanding its function and how it interacts with host cells particularly valuable.
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 Validation Studies
Researchers can use this recombinant C. trachomatis OmpA protein as an immunogen to create polyclonal or monoclonal antibodies against the major outer membrane porin. The dual-tag design—with its N-terminal His-tag and C-terminal Myc-tag—simplifies both purification and detection during antibody screening. Since the expressed mature protein region (23-394aa) represents the native antigenic surface that appears during natural infections, it may produce antibodies that recognize native epitopes effectively. Scientists could then validate these antibodies through Western blot, ELISA, or immunofluorescence assays using the recombinant protein.
2. Protein-Protein Interaction Studies
Pull-down assays can take advantage of this dual-tagged recombinant OmpA to hunt for potential binding partners or host cell receptors that might interact with C. trachomatis outer membrane components. The N-terminal His-tag works well for attachment to nickel-based affinity matrices, while the C-terminal Myc-tag offers another way to detect the protein and check its integrity during interaction experiments. Researchers can incubate cell lysates or purified candidate proteins with immobilized OmpA to look for specific binding interactions under controlled laboratory conditions.
3. Immunological Assay Development
This recombinant protein may serve as a standardized antigen for creating and fine-tuning various immunoassays, including ELISA-based detection systems and immunoblotting protocols. The >85% purity level should be adequate for use as a coating antigen or positive control in serological research. The dual-tag system helps with assay development by offering multiple detection approaches and allowing precise measurement of protein loading in experimental setups.
4. Biochemical Characterization Studies
Scientists can subject the purified recombinant OmpA protein to various biochemical analyses to examine its physicochemical properties—things like thermal stability, pH sensitivity, and how it behaves in different detergents. Size exclusion chromatography and dynamic light scattering experiments might reveal insights into the protein's oligomerization state and whether it tends to aggregate under different buffer conditions. These studies could help build a better understanding of this important chlamydial surface protein's basic biochemical behavior in controlled laboratory settings.
