Recombinant Human Uridine-cytidine kinase 1 (UCK1) is produced in an E. coli expression system and contains the complete sequence of isoform 2, covering amino acids 1-201. The protein includes an N-terminal 6xHis-SUMO tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms purity levels above 90%, and the product appears well-suited for research applications where consistent experimental performance is needed.
Uridine-cytidine kinase 1 (UCK1) is an enzyme with a key function in the pyrimidine salvage pathway. It catalyzes the phosphorylation of uridine and cytidine, converting them to their respective monophosphate forms. This process seems essential for nucleotide metabolism and may help maintain proper cellular nucleotide pools. UCK1 has drawn particular attention from researchers studying nucleotide synthesis and how cells regulate these pathways in different contexts.
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. Enzyme Kinetics and Substrate Specificity Studies
This recombinant UCK1 protein allows researchers to examine the kinetic parameters and substrate preferences of human uridine-cytidine kinase 1 under controlled laboratory conditions. Scientists can measure enzyme activity using different nucleoside substrates like uridine and cytidine to calculate Km and Vmax values. The high purity (>90%) should provide reliable kinetic measurements while minimizing interference from contaminating proteins. The N-terminal His-SUMO tag makes purification simpler and enables immobilization for continuous assay formats.
2. Nucleotide Analog Drug Metabolism Research
Researchers may find this recombinant UCK1 useful for studying how nucleoside analogs are phosphorylated, particularly those being developed for antiviral and anticancer treatments. Scientists can explore whether structural changes to nucleoside substrates influence how well UCK1 recognizes and phosphorylates them. This application could prove especially valuable for understanding how therapeutic nucleoside analogs become metabolically activated during preclinical drug development. The purified enzyme permits controlled assessment of analog processing without the complications that whole cells might introduce.
3. Protein-Protein Interaction Studies
The His-SUMO tagged UCK1 can work as bait in pull-down assays designed to identify potential binding partners or regulatory proteins that might interact with uridine-cytidine kinase 1. The dual tagging system offers flexibility for various purification and detection approaches in interaction studies. Scientists can deploy this protein in biochemical assays to better understand UCK1's position within cellular nucleotide metabolism networks. High expression levels from E. coli should provide adequate protein quantities for thorough interaction screening experiments.
4. Antibody Development and Validation
This recombinant UCK1 protein appears to be an excellent antigen for creating specific antibodies against human uridine-cytidine kinase 1. The complete isoform 2 sequence (1-201aa) offers full epitope coverage, which may be ideal for polyclonal antibody production or monoclonal antibody screening. Researchers can test antibody specificity using this purified protein through Western blotting, ELISA, and other immunoassays. The high purity level suggests that any antibodies generated will likely target UCK1 specifically rather than contaminating proteins.
5. Structural and Biophysical Characterization
Scientists can apply this purified recombinant UCK1 in biophysical studies aimed at understanding protein folding, stability, and conformational changes that occur when substrates or inhibitors bind. Techniques such as circular dichroism spectroscopy, dynamic light scattering, or differential scanning fluorimetry might reveal important details about the protein's structural properties. The His-SUMO tag can be removed when structural studies require native protein termini. These investigations may provide fundamental insights into how UCK1's structure relates to its function in nucleotide metabolism.
