Recombinant Human Glutathione S-transferase P (GSTP1) is produced in a yeast expression system, which appears to ensure high fidelity of protein folding and stability. The full-length mature protein spans amino acids 2 to 210. It comes with an N-terminal 10xHis-tag that makes purification and detection in research applications more straightforward. SDS-PAGE verification shows the purity exceeds 90%, suggesting this protein may be a reliable tool for biochemical assays and experimental studies.
Glutathione S-transferase P (GSTP1) belongs to the glutathione S-transferase family. These enzymes seem to play a crucial role in detoxifying both endogenous and exogenous compounds through conjugation with glutathione. GSTP1 is likely involved in cellular processes like detoxification and protection against oxidative stress. This makes it a significant focus in research related to cancer, drug resistance, and toxicology 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. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
The N-terminal 10xHis tag on this recombinant GSTP1 allows for nickel-affinity based pull-down experiments to identify potential binding partners or substrates. Researchers can immobilize the protein on nickel-coated beads or columns, then incubate it with cell lysates or purified protein libraries to capture interacting molecules. This approach appears particularly valuable for studying GSTP1's role in cellular detoxification pathways and identifying novel regulatory proteins. The >90% purity should minimize background binding from contaminant proteins during interaction studies.
2. Antibody Development and Validation
This recombinant GSTP1 can serve as an immunogen for generating specific antibodies against human GSTP1. It also works as a positive control for validating existing antibodies. The full-length mature protein (aa 2-210) provides complete antigenic epitopes for comprehensive antibody screening. High purity (>90%) suggests that generated antibodies will likely be specific to GSTP1 rather than contaminating proteins. The His-tag can also be used in ELISA-based antibody characterization assays using anti-His detection systems.
3. Biochemical Characterization and Enzyme Kinetics Studies
While biological activity hasn't been tested, this recombinant protein may be used to establish and optimize activity assays for glutathione S-transferase function. Standard GST substrates like CDNB (1-chloro-2,4-dinitrobenzene) could work for this purpose. Researchers can assess the protein's structural integrity through various biochemical techniques including circular dichroism spectroscopy and thermal stability assays. Once activity is confirmed, kinetic parameters and substrate specificity can be determined, potentially providing valuable data for understanding GSTP1 function in detoxification processes.
4. Inhibitor Screening and Drug Discovery Research
This recombinant GSTP1 might be used in high-throughput screening assays to identify potential inhibitors or modulators of glutathione S-transferase activity. The His-tag makes protein immobilization for screening platforms easier. High purity should reduce interference in optical or fluorescence-based detection systems. Compound libraries can be tested for their effects on GSTP1 function, which may contribute to developing research tools for studying cellular detoxification mechanisms.
