Recombinant Human Corticotropin-releasing factor receptor 1 (CRHR1) gets produced through an E. coli expression system and represents a partial protein segment spanning amino acids 24 to 121. The protein carries an N-terminal GST tag to help with purification and detection. SDS-PAGE analysis confirms the product maintains a purity level above 90%, which appears to provide good reliability for research work. This product is meant strictly for research use and cannot be used for therapeutic purposes.
CRHR1 seems to be a key player in the corticotropin-releasing hormone signaling pathway. The receptor likely plays an important role in how we handle stress by controlling the hypothalamic-pituitary-adrenal (HPA) axis. This makes CRHR1 particularly interesting for scientists studying stress responses, brain function, and hormone systems - offering a useful target for research into the molecular details of these complex 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 CRHR1 fragment (24-121aa) may work well as an immunogen or antigen when developing antibodies against the extracellular domain of human CRHR1. The N-terminal GST tag makes purification and immobilization easier for immunization procedures or screening tests. That >90% purity suggests it could generate antibodies that specifically recognize the natural receptor. Scientists might use this protein in ELISA-based screening to find high-affinity antibodies. They could also test antibody specificity through competitive binding experiments.
2. GST Pull-Down Assays for Protein-Protein Interactions
The N-terminal GST tag allows direct use in GST pull-down experiments to hunt down potential binding partners of the CRHR1 extracellular domain. Scientists can attach the protein to glutathione-sepharose beads, then mix it with cell lysates or purified proteins to grab interacting molecules. This method appears particularly useful for studying how receptors and ligands interact, or for discovering new binding partners within that 24-121 amino acid stretch. The high purity (>90%) should minimize unwanted background binding from contaminating proteins.
3. Biochemical Characterization and Binding Studies
Scientists can use this CRHR1 fragment in direct binding assays to study how it interacts with known ligands like corticotropin-releasing factor (CRF) or similar peptides. The purified protein makes dose-response studies possible, along with detailed analysis of how quickly ligands bind to the extracellular domain. Researchers might run competition assays with different CRF variants to figure out exactly where binding happens within this receptor region. The GST tag provides a handy anchor point for attaching the protein in surface plasmon resonance experiments or other binding assays that don't need labels.
4. ELISA-Based Screening and Detection Assays
The GST-tagged CRHR1 fragment could work as either a capture or detection tool in enzyme-linked immunosorbent assays for research purposes. Scientists can coat the protein directly onto ELISA plates or capture it using anti-GST antibodies to build standardized assays for measuring receptor-ligand interactions. This setup may help with screening small molecule libraries or testing peptide variants for binding to the CRHR1 extracellular domain. The high purity level suggests consistent assay performance and repeatable results across different experiments.
