Recombinant Plasmodium falciparum Glutathione S-transferase (GST) gets expressed in a yeast system, covering amino acids 1-211 of the full-length protein. The product includes an N-terminal 10xHis-tag that makes purification and detection more straightforward. SDS-PAGE analysis shows this recombinant protein achieves over 85% purity, which appears to meet high-quality standards for research applications. This product is designed strictly for research use and meets rigorous specifications for reliable experimental outcomes.
Glutathione S-transferase (GST) from Plasmodium falciparum likely plays a crucial role in how the parasite handles detoxification. The protein works by catalyzing glutathione conjugation to various substrates, which helps neutralize toxic compounds. This makes GST particularly significant for research aimed at understanding how the parasite survives and for developing potential malaria interventions.
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.
The recombinant Plasmodium falciparum Glutathione S-transferase (GST, 1–211aa) expressed in yeast with an N-terminal 10×His tag represents the full-length enzyme, and yeast is a suitable eukaryotic system for expressing soluble cytosolic enzymes such as GST. Because GST is a well-folded, dimeric enzyme that does not rely on complex post-translational modifications, there is a high probability that the recombinant protein is correctly folded and enzymatically active. Yeast can produce properly folded, soluble GST with native-like activity, although this must still be experimentally verified through enzymatic assays (e.g., using CDNB substrates).
1. Biochemical Characterization and Enzyme Kinetics Studies
This recombinant P. falciparum GST can be used to study enzymatic properties and substrate specificity through in vitro assays measuring kinetic parameters such as Km and Vmax with glutathione-conjugating substrates. If the protein retains correct folding and dimerization, it should display measurable GST activity suitable for mechanistic characterization. If misfolded or partially inactive, it may still serve for qualitative substrate binding or comparative analyses, but not for accurate kinetic modeling. Thus, functional validation through enzymatic assays should precede kinetic studies.
2. Drug Resistance Mechanism Research
The recombinant GST is useful for exploring drug resistance mechanisms related to oxidative stress and detoxification in P. falciparum. Researchers can analyze how GST interacts with antimalarial compounds or their metabolites. If the enzyme is correctly folded and active, it can provide meaningful data on drug conjugation or detoxification activity. If inactive, it may still serve for binding or inhibition screening but not for functional resistance modeling. Therefore, enzymatic validation is essential to confirm its biological relevance in resistance mechanism studies.
3. Antibody Development and Immunological Studies
The His-tagged GST protein is suitable for producing P. falciparum GST-specific antibodies. The >85% purity supports consistent immunogenicity. If folded correctly, antibodies developed from this antigen may recognize both native and denatured GST in parasite samples. If misfolded, it can still generate linear-epitope antibodies, effective for Western blotting and ELISA but not necessarily for recognizing native epitopes in immunofluorescence or immunoprecipitation. Thus, it is a valid antigen, though conformational validation enhances its utility for native detection studies.
4. Protein-Protein Interaction Studies
The recombinant GST can be used to identify potential binding partners in the P. falciparum proteome or host cell extracts using pull-down or affinity capture methods. If folded correctly, its native dimeric structure will support physiologically relevant interactions. If misfolded, binding assays may still detect nonspecific or partial interactions, requiring caution in data interpretation. Therefore, results from interaction studies should be corroborated with additional biophysical or cellular assays.
5. Comparative Enzymology and Evolution Studies
The recombinant P. falciparum GST is appropriate for comparative studies with GSTs from other Plasmodium species or organisms to assess evolutionary and functional differences. If correctly folded, it enables accurate cross-species comparison of enzyme kinetics, substrate range, and catalytic efficiency. If partially misfolded, it can still contribute to structural sequence-based comparisons but not to quantitative enzymatic analyses. Folding and activity verification should be confirmed before detailed comparative studies.
