Recombinant Mouse Pyridoxal phosphate phosphatase (Pdxp) is produced in a yeast system, which appears to provide efficient and reliable results. The full-length protein covers amino acids 1 to 292 and includes an N-terminal 6xHis tag that makes purification and detection more straightforward. SDS-PAGE analysis confirms purity levels above 90%, though this protein is intended specifically for research applications where high-quality reagents matter most.
Pyridoxal phosphate phosphatase (Pdxp) is an enzyme that removes phosphate groups from pyridoxal 5'-phosphate (PLP), the active form of vitamin B6. It likely plays an important role in controlling PLP levels, which are essential for many metabolic pathways. Research on Pdxp may reveal new insights into how metabolic processes are regulated and how enzymes function, making it a useful tool for biochemistry and physiology studies.
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. Biochemical Characterization of Pyridoxal Phosphate Phosphatase Activity
This recombinant mouse Pdxp protein can help establish in vitro enzyme assays to study its phosphatase activity against pyridoxal phosphate and related vitamin B6 compounds. The N-terminal 6xHis tag makes protein purification easier and allows for immobilization during kinetic studies. Researchers can determine which substrates the enzyme prefers, find optimal reaction conditions, and measure kinetic parameters. These biochemical studies would provide basic insights into how vitamin B6 metabolism is regulated in mouse models.
2. Antibody Development and Validation Studies
The purified recombinant protein works well as an antigen for creating specific antibodies against mouse Pdxp through standard immunization methods. High purity levels (>90%) should minimize unwanted cross-reactions with other proteins during antibody production. These antibodies could then be tested using the same recombinant protein in Western blots, ELISA, or immunoprecipitation experiments to verify specificity and binding strength.
3. Protein-Protein Interaction Studies
The 6xHis-tagged recombinant Pdxp can be used in pull-down experiments to find potential protein partners involved in vitamin B6 metabolism. The protein can be attached to nickel-affinity beads and mixed with mouse tissue extracts or cell lysates to capture interacting proteins. This method might uncover new regulatory mechanisms or metabolic complexes that involve pyridoxal phosphate phosphatase.
4. Structural and Biophysical Analysis
This full-length recombinant protein provides adequate material for structural studies, including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to determine the three-dimensional structure of mouse Pdxp. The purified protein can also be analyzed using biophysical methods such as dynamic light scattering, circular dichroism spectroscopy, or thermal stability tests to understand protein folding, stability, and structural changes under various conditions.
5. Comparative Species Analysis
The mouse-specific recombinant Pdxp allows for comparative studies with similar proteins from other species to examine evolutionary conservation and functional differences in vitamin B6 metabolism. Comparing enzyme activity across species, analyzing structural similarities, and studying substrate preferences using this mouse protein alongside human or other mammalian versions could provide insights into species-specific metabolic differences and regulatory systems.
