Recombinant Pan troglodytes Lymphotoxin-beta (LTB) is produced using an E. coli expression system, covering the 49-244 amino acid region of the extracellular domain. The protein carries an N-terminal 6xHis-SUMO tag to simplify purification and analysis. SDS-PAGE confirms the product shows greater than 90% purity, which appears suitable for various research applications. This recombinant protein is designed for research use only and is not intended for therapeutic or diagnostic purposes.
Lymphotoxin-beta (LTB) plays a central role in the immune system, mainly through signaling pathways that control lymphoid tissue development and organization. It belongs to the tumor necrosis factor superfamily and seems crucial for maintaining the structure of secondary lymphoid organs. LTB's involvement in immune response regulation has made it an important target in immunology research, especially in studies exploring lymphoid organogenesis and immune system development.
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. Comparative Evolutionary Protein Structure Analysis
This recombinant chimpanzee LTB extracellular domain may help researchers study how lymphotoxin-beta structure has been conserved or changed between Pan troglodytes and other primate species. The purified protein allows for detailed biochemical characterization - techniques like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation can determine folding patterns and oligomerization states. When compared with human LTB, structural studies might reveal species-specific conformational differences that evolved between closely related primates. The N-terminal His-SUMO tag makes purification and immobilization easier for structural analysis techniques.
2. Cross-Species Protein-Protein Interaction Studies
The His-SUMO tagged chimpanzee LTB extracellular domain works well as a tool for pull-down assays. Researchers can identify and characterize potential binding partners from chimpanzee or human cell lysates. The recombinant protein can be immobilized on nickel-affinity resins to capture interacting proteins, which are then identified through mass spectrometry analysis. This approach helps investigate whether chimpanzee LTB maintains similar binding specificities compared to human orthologs and could reveal novel interaction networks. The high purity level appears to reduce background binding in these interaction studies.
3. Antibody Development and Cross-Reactivity Testing
This recombinant chimpanzee LTB can serve as an immunogen for generating species-specific antibodies. It's also useful for testing cross-reactivity of existing anti-human LTB antibodies. The purified extracellular domain represents the native antigenic surface that would be exposed under physiological conditions, making it appropriate for antibody screening applications. ELISA-based assays using the His-tagged protein can be developed to characterize antibody binding kinetics and specificity. Such antibodies would likely prove valuable as research tools for studying chimpanzee immune system components in comparative immunology research.
4. Protein Stability and Folding Studies
The recombinant chimpanzee LTB extracellular domain provides a model system for investigating protein stability and folding mechanisms within the lymphotoxin family. Thermal denaturation studies, chemical unfolding experiments, and refolding kinetics can be performed to characterize the thermodynamic properties of this primate protein variant. The SUMO tag can be cleaved when needed to study native protein behavior, while the His tag makes purification of properly folded protein straightforward for these biophysical analyses. These studies may contribute to understanding structure-stability relationships in cytokine family proteins across species.
