Recombinant Bovine Odorant-binding Protein is expressed in a baculovirus system and includes an N-terminal 10xHis-tag for easy purification. The protein is produced as a full-length sequence from amino acids 1 to 159 and achieves a purity level greater than 85% as determined by SDS-PAGE analysis. This product is designed for research use only and provides reliable performance in various experimental applications.
Odorant-binding proteins from Bos taurus appear to play a critical role in the olfactory system by binding and transporting volatile odor molecules. These proteins seem essential in the initial steps of odor detection and signal transduction. This makes them an intriguing subject of study in olfactory research and the broader field of sensory biology.
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. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
The N-terminal 10xHis-tag allows immobilization of the recombinant bovine odorant-binding protein on nickel-affinity matrices for pull-down experiments. Researchers might use this approach to identify potential binding partners or interacting proteins from bovine tissue lysates or purified protein libraries. The 85% purity level is likely sufficient for these interaction studies, since the His-tag provides specific capture while contaminants can be washed away during the procedure.
2. Antibody Development and Validation
The recombinant protein may serve as an immunogen for generating polyclonal or monoclonal antibodies specific to bovine odorant-binding protein. The baculovirus expression system typically provides proper protein folding and post-translational modifications, which suggests it could be suitable for producing antibodies that recognize the native protein. Scientists can also use the His-tag in ELISA-based screening and validation of antibody specificity during the development process.
3. Biochemical Characterization and Stability Studies
Researchers can subject the purified protein to various biochemical analyses including thermal stability assays, pH tolerance studies, and buffer optimization experiments. Such studies would provide fundamental information about the protein's biophysical properties and optimal storage conditions. The relatively high purity level allows for reliable spectroscopic measurements and other analytical techniques to characterize the protein's behavior under different experimental conditions.
4. Comparative Protein Analysis Across Species
This bovine odorant-binding protein can be used in comparative studies alongside odorant-binding proteins from other species to investigate evolutionary relationships and structural differences. SDS-PAGE analysis, Western blotting, and cross-reactivity studies with antibodies raised against odorant-binding proteins from different species may provide insights into conserved and divergent features within this protein family.
