Recombinant Human Triggering receptor expressed on myeloid cells 2 (TREM2) is produced in E. coli and contains amino acids 19-174. This partial protein features an N-terminal 10xHis-GST tag along with a C-terminal Myc tag, which makes purification and detection more straightforward. The protein achieves purity greater than 85% based on SDS-PAGE analysis, suggesting it should work reliably in research settings.
TREM2 appears to be a receptor found mainly on myeloid cells. It seems to play an important role in immune system function, particularly in controlling inflammatory responses. Researchers studying neurodegenerative diseases and innate immunity have shown considerable interest in this receptor. Learning how TREM2 works and what regulates it may prove essential for scientists investigating its role in different cellular pathways and disease processes.
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. Antibody Development and Validation
This recombinant TREM2 extracellular domain (19-174aa) could work as an immunogen or screening antigen when developing monoclonal or polyclonal antibodies against human TREM2. The dual tagging approach with N-terminal His-GST and C-terminal Myc tags offers flexible detection and purification options during antibody characterization. Researchers can run ELISA-based screening assays with this protein to find antibodies that bind specifically and strongly to the TREM2 extracellular region. Cross-reactivity testing is possible using this recombinant protein to confirm antibody specificity before moving to more complicated experimental systems.
2. Protein-Protein Interaction Studies
Scientists can use the recombinant TREM2 extracellular domain in pull-down assays to hunt for potential binding partners or ligands that interact with this part of TREM2. The N-terminal His-GST tag makes it easier to attach the protein to appropriate matrices for affinity purification experiments with cell lysates or purified protein libraries. Since the purity level exceeds 85%, this should give reliable results in biochemical binding assays while reducing unwanted background signals. Surface plasmon resonance or similar biophysical methods may work well with this protein to measure how fast and how tightly known or suspected TREM2 interacting molecules bind.
3. Structural and Biochemical Characterization
This recombinant protein offers a dependable foundation for studying the structural features and biochemical properties of the TREM2 extracellular domain. Scientists can analyze it using circular dichroism spectroscopy, dynamic light scattering, or other biophysical approaches to check protein folding, stability, and whether it forms complexes. Proteolytic mapping experiments are feasible to pinpoint accessible areas and possible cleavage sites within the extracellular domain. Having two different tags provides multiple options for purification and detection during structural research.
4. ELISA-Based Detection Assays
The dual-tagged TREM2 protein works well as a standard or control in sandwich ELISA assays meant to detect TREM2 or its fragments in biological samples. Both Myc and His-GST tags supply multiple binding sites for capture or detection antibodies, giving researchers flexibility in assay setup. This recombinant protein helps establish standard curves for quantitative measurements and confirms that TREM2 detection systems work as intended. The known concentration and purity make it appropriate for creating consistent calibration standards in research.
5. Cell-Based Binding and Uptake Studies
Scientists can use the recombinant TREM2 extracellular domain in cell culture experiments to explore how cells bind, take up, or transport molecules. The protein can be labeled with fluorescent markers or detected through its tags to track interactions with cells that express TREM2 receptors or binding partners. Competition experiments using this recombinant protein may help determine how specific these cellular interactions really are. The reliable expression in E. coli and high purity level should produce consistent results across repeated experiments in cell-based research.
