Recombinant Yersinia enterocolitica Protein YopB is produced in E. coli and includes an N-terminal 6xHis-tag, which simplifies the purification process. This product represents a partial expression region spanning amino acids 1-165. The protein comes with purity levels above 85%, verified through SDS-PAGE analysis. Intended strictly for research purposes, this recombinant protein lacks endotoxin information.
YopB appears to be a crucial element of the Type III secretion system in Yersinia enterocolitica. It likely plays a central role in moving effector proteins into host cells. The protein seems essential for the bacterium's ability to cause disease, which makes it an attractive target for investigating bacterial infection pathways and possibly developing 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 Immunological Studies
This recombinant YopB fragment may work well as an immunogen for creating polyclonal or monoclonal antibodies that specifically target Yersinia enterocolitica YopB protein. The N-terminal 6xHis tag makes purification straightforward and helps with immobilization during antibody screening assays. These antibodies could prove useful as research tools for examining YopB expression, where it localizes, and how it functions in bacterial disease studies. The partial protein sequence (1-165aa) covers a substantial portion that might harbor important antigenic sites for antibody binding.
2. Protein-Protein Interaction Studies
The 6xHis tag allows for pull-down experiments to find potential host cell proteins that bind to the YopB N-terminal region when Yersinia infects cells. Researchers can attach the recombinant protein to nickel-affinity resins and mix it with host cell extracts to catch interacting partners. This method could shed light on how YopB contributes to bacterial harm and manipulates host cells at the molecular level. The 85% purity appears adequate for these interaction experiments while reducing interference from unwanted proteins.
3. ELISA-Based Binding Assays
The His-tagged YopB fragment works in enzyme-linked immunosorbent assays to examine binding with different ligands or to test potential small molecule blockers. The protein can be placed directly on ELISA plates or captured using anti-His antibodies for uniform positioning. This approach proves particularly helpful for studying how specifically the YopB N-terminal domain binds and for measuring the timing of molecular interactions. The partial protein length offers a well-defined region for targeted binding research.
4. Biochemical Characterization and Stability Studies
This recombinant protein serves as a reasonable starting material for biochemical analysis, including heat stability, pH resistance, and sensitivity to protein-cutting enzymes in the YopB N-terminal region. The specific expression region (1-165aa) makes it possible to compare systematically with other YopB versions or similar proteins from different Yersinia species. Studies like these can reveal what structural features YopB needs to work properly and may help pinpoint critical amino acids within this region.
