Recombinant Human Glutathione S-transferase P (GSTP1) is expressed in E. coli and comprises the full length of the mature protein (amino acids 2-210). It features an N-terminal 6xHis tag for ease of purification and detection. The protein is purified to greater than 90% purity, as confirmed by SDS-PAGE analysis, ensuring high-quality standards for research applications.
GSTP1 belongs to the glutathione S-transferase family and appears to play a crucial role in cellular detoxification processes. The enzyme catalyzes the conjugation of glutathione to various electrophilic compounds, which may help with xenobiotic metabolism and protection against oxidative stress. Researchers often examine GSTP1 for its role in cellular defense mechanisms, though its broader implications in different research contexts continue to emerge.
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. Glutathione Conjugation Assays and Enzyme Kinetics Studies
This recombinant GSTP1 protein works well for investigating the enzyme's catalytic properties through in vitro glutathione conjugation assays with various electrophilic substrates. Kinetic parameters such as Km and Vmax values can be determined for different substrate combinations, potentially revealing insights into the enzyme's specificity and efficiency. The high purity (>90%) likely ensures reliable and reproducible results in biochemical characterization studies. That N-terminal 6xHis tag makes purification straightforward and allows for immobilization in continuous assay systems.
2. Protein-Protein Interaction Studies
The recombinant GSTP1 may serve as an effective target protein in pull-down assays to identify novel binding partners or validate known interactions with other cellular proteins. The N-terminal 6xHis tag allows for efficient capture with nickel-affinity resins, letting researchers isolate protein complexes from cell lysates or test direct interactions with purified proteins. This approach could help clarify GSTP1's role in cellular signaling pathways beyond its catalytic function. Surface plasmon resonance or other biophysical techniques can also quantify binding affinities and kinetics, though results may vary depending on experimental conditions.
3. Antibody Development and Validation
This full-length mature GSTP1 protein works as an antigen for generating specific antibodies against human GSTP1 in preclinical research settings. The recombinant protein can immunize laboratory animals for polyclonal antibody production. It also serves as a screening antigen for monoclonal antibody development. Antibody specificity and cross-reactivity can be validated using this purified protein in ELISA, Western blot, and other immunoassays. The high purity minimizes background interference during antibody characterization studies, though some non-specific binding may still occur.
4. Structural Biology and Biophysical Characterization
The purified recombinant GSTP1 protein proves useful for structural studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to understand its three-dimensional architecture. Biophysical techniques such as dynamic light scattering, circular dichroism spectroscopy, and thermal stability assays can provide insights into protein folding, stability, and conformational changes. If needed for structural studies requiring native protein termini, the N-terminal His tag can be removed enzymatically. These studies contribute to understanding structure-function relationships and may inform rational drug design approaches.
5. Inhibitor Screening and Drug Discovery Research
This recombinant GSTP1 protein can be used in high-throughput screening assays to identify potential small molecule inhibitors for research purposes. Enzyme-based assays with this protein can test compound libraries and evaluate inhibitory potency through IC50 determinations. Structure-activity relationship studies using this protein may help optimize lead compounds and understand inhibition mechanisms. The consistent quality and purity of the recombinant protein appears to support reproducible results across different screening campaigns and research laboratories.
