This recombinant human rhodopsin (RHO) protein comes from E. coli expression and covers amino acids 1-36 of the full protein. The fragment carries an N-terminal 6xHis-SUMO tag, which makes purification and detection much more straightforward. SDS-PAGE analysis shows the protein achieves greater than 90% purity—a level that should deliver reliable results for most research work.
Rhodopsin acts as a light-sensitive receptor that plays a central role in visual phototransduction. The protein handles the critical job of converting light into electrical signals within the retina. Because rhodopsin sits at the heart of vision, studying it may help researchers better understand how we see and what goes wrong in various visual disorders. This makes it a particularly valuable target for sensory biology 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 Validation
This N-terminal rhodopsin fragment (amino acids 1-36) appears well-suited for creating antibodies that specifically recognize the N-terminal region. The 6xHis-SUMO tag offers extra epitopes while simplifying purification steps needed for immunization work. Scientists can likely use this fragment to produce either monoclonal or polyclonal antibodies for Western blots, immunoprecipitation experiments, or immunofluorescence studies focused on rhodopsin. With purity above 90%, contamination that might cause unwanted cross-reactivity should be minimal.
2. Protein-Protein Interaction Studies
Pull-down experiments may benefit from using rhodopsin's N-terminal domain to fish out binding partners that specifically interact with this region. The N-terminal 6xHis tag makes it easy to attach the protein to nickel-affinity resins, letting researchers capture potential partners from cell lysates or purified protein collections. This strategy could shed light on how rhodopsin's N-terminus contributes to protein complex assembly and cellular signaling networks.
3. ELISA-Based Binding Assays
The tagged rhodopsin fragment works well for developing enzyme-linked immunosorbent assays to study molecular interactions or screen compound libraries. Since the 6xHis tag allows controlled attachment to nickel-coated plates, the rhodopsin fragment gets presented in a uniform way for binding experiments. Researchers might find this system useful for examining binding kinetics, specificity, and how tightly various ligands or proteins stick to rhodopsin's N-terminal region.
4. Biochemical Characterization and Stability Studies
This purified fragment gives researchers a clean starting point for analyzing N-terminal domain properties—things like thermal stability, how it responds to pH changes, and whether it's vulnerable to protein-cutting enzymes. The SUMO tag appears to boost protein stability and solubility, which could prove helpful for biophysical techniques like dynamic light scattering, circular dichroism spectroscopy, or analytical ultracentrifugation. Such experiments might reveal important details about how rhodopsin's N-terminal region behaves structurally under different laboratory conditions.
