Recombinant Human Phospholipid transfer protein (PLTP) is produced using a yeast expression system and includes the complete mature protein sequence from amino acids 18 to 493. The protein carries an N-terminal 6xHis tag for easier purification and detection. SDS-PAGE analysis confirms purity levels above 90%, which appears suitable for different experimental uses. This product is intended for research purposes only.
Phospholipid transfer protein (PLTP) seems to play a central role in how the body handles lipid metabolism. The protein is involved in moving phospholipids between lipoproteins and participates in reshaping high-density lipoproteins (HDL). It also influences cholesterol efflux processes. Given its role in lipid transport and metabolism, PLTP has become an important target for cardiovascular and metabolic research.
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.
Based on the provided information, the folding state and bioactivity of this recombinant PLTP protein are unknown and cannot be assumed. PLTP is a lipid-transfer protein that requires specific folding to form its lipid-binding pocket and mediate its function in phospholipid transfer. While the protein is expressed as the full-length mature sequence (18-493aa) in a yeast expression system (which can provide some eukaryotic post-translational modifications), the presence of an N-terminal 6xHis tag could potentially interfere with the protein's N-terminal structure or function. The >90% purity indicates minimal contaminants but does not confirm correct folding or lipid-transfer activity. Therefore, applications that depend on the protein's specific biological activity or native conformation are speculative without experimental validation.
1. Antibody Development and Immunoassay Optimization
This recombinant PLTP is suitable for use as an immunogen to generate antibodies. The full-length sequence provides multiple epitopes for antibody recognition. While the full-length protein provides linear epitopes, antibodies generated may not recognize conformational epitopes of the native, lipid-bound PLTP in human plasma unless the recombinant PLTP protein is correctly folded. The recombinant PLTP protein is reliable for developing antibodies that work in techniques like Western blotting, but their ability to recognize functional PLTP in its native state requires validation.
2. Protein-Protein Interaction Studies Using His-Tag Affinity
The His-tagged recombinant PLTP can be immobilized for pull-down experiments. However, the utility for identifying biological interaction partners is contingent upon correct folding. PLTP's interactions with lipoproteins (e.g., HDL) and other factors are conformation-dependent. If the recombinant PLTP protein is misfolded, it may not present the correct binding surfaces, leading to the identification of non-specific interactors. This approach should be considered exploratory until protein activity is confirmed.
3. Biochemical Characterization and Stability Studies
This purified recombinant PLTP is well-suited for biochemical characterization, including thermal stability, pH tolerance, and oligomerization state studies. This application is valid as it focuses on intrinsic physical properties independent of bioactivity. These studies will characterize the properties of this specific recombinant PLTP protein, not the native PLTP.
4. ELISA Development and Quantitative Detection Assays
The His-tagged recombinant PLTP protein can be used in ELISA development. However, its suitability as a standard for "measuring endogenous PLTP levels in biological samples" is limited. An ELISA built with this reagent may not accurately quantify native PLTP in plasma if the recombinant PLTP protein lacks proper folding or post-translational modifications present in the circulating protein. It is most reliable for detecting antibodies against the immunogen itself or for quality control of the recombinant PLTP protein.
Final Recommendation & Action Plan
The immediate priority is to validate the phospholipid transfer activity of this recombinant PLTP using a standard assay (e.g., measuring the transfer of fluorescently-labeled phospholipids between liposomes) before investing in functional studies. If activity is confirmed, the protein becomes valuable for interaction studies (Application 2) and as a standard in functional assays. If inactive, its use should be restricted to antibody production (Application 1) and biochemical characterization (Application 3). For Application 4 (ELISA development), the assay should be validated against a gold standard method using native PLTP from human plasma to ensure accurate quantification. The yeast expression system may not provide the same glycosylation patterns as human cells, which could affect antibody recognition in immunoassays.
