Recombinant Human F-box only protein 48 (FBXO48) is expressed in E. coli, spanning the complete protein sequence from amino acids 1-155. The construct includes an N-terminal 10xHis tag and a C-terminal Myc tag, which streamline purification and detection processes. SDS-PAGE analysis confirms the protein achieves greater than 90% purity, suggesting strong reliability for research applications. This protein is strictly for research use and should not be applied for diagnostic or therapeutic purposes.
FBXO48 belongs to the F-box protein family, which appears to play a crucial role in the ubiquitin-proteasome system. These F-box proteins act as essential components of the SCF (SKP1-Cullin-F-box) complex, where they function as substrate recognition units. Through its role in protein degradation, FBXO48 likely contributes to cellular processes including cell cycle regulation and signal transduction. This makes it a compelling target for researchers studying cellular homeostasis and related pathways.
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 Pull-Down Assays
The dual-tagged design of FBXO48—with both N-terminal His-tag and C-terminal Myc-tag—opens up comprehensive protein interaction mapping through pull-down experiments. Researchers can immobilize the protein on nickel-affinity resins via the His-tag to capture potential binding partners from cell lysates or purified protein libraries. Meanwhile, the Myc-tag offers an additional detection route for Western blot confirmation and may serve as an alternative capture method using anti-Myc antibodies. This dual-tag approach provides experimental flexibility and built-in validation opportunities when hunting for novel FBXO48 interacting proteins.
2. Antibody Development and Validation
The high-purity recombinant FBXO48 protein (>90% pure) makes an excellent immunogen for creating specific antibodies against this F-box protein. Since the full-length construct (1-155aa) retains native epitopes found in endogenous FBXO48, it appears well-suited for producing antibodies with physiological relevance. Both polyclonal and monoclonal antibody development can take advantage of this purified protein. The dual tags also provide convenient built-in controls for specificity testing and cross-reactivity assessment during antibody characterization.
3. Biochemical Characterization and Stability Studies
Purified FBXO48 protein allows for detailed biochemical analysis, including thermal stability profiling, pH tolerance testing, and buffer optimization studies. These experiments can help establish optimal storage and handling conditions while revealing insights into the protein's biophysical properties. The dual-tag system enables consistent protein detection and quantification throughout stability studies—researchers can choose between His-tag detection or Myc-tag immunodetection methods depending on their experimental needs.
4. ELISA-Based Quantitative Assays
The Myc-tagged FBXO48 protein can be adapted to develop sandwich or competitive ELISA assays for research applications. The Myc epitope provides a dependable detection mechanism using commercially available anti-Myc antibodies, while the protein can be immobilized either through its His-tag or through direct coating methods. Such assays might prove valuable for screening compound libraries or investigating factors that influence FBXO48 levels in experimental systems.
