Recombinant Mouse Neuropeptide Y receptor type 2 (Npy2r) gets produced in E. coli and contains a partial protein sequence spanning amino acids 1 to 51. The recombinant protein comes with an N-terminal 10xHis-tag that helps with purification and detection. SDS-PAGE analysis confirms the product reaches a purity level above 85%, which appears to make it a solid reagent for research work. This product is strictly for research purposes—not for clinical or diagnostic applications.
Neuropeptide Y receptor type 2 (Npy2r) seems to be a key player in the neuropeptide Y signaling pathway. This pathway likely influences several physiological processes, including how we regulate appetite, experience anxiety, and maintain circadian rhythms. Since Npy2r functions as a G-protein-coupled receptor, it probably modulates intracellular signaling cascades. Neuroscience and metabolic researchers find this receptor particularly interesting. Getting a better grasp of how it works may help us understand more complex biological responses and underlying mechanisms.
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 N-terminal fragment of mouse Npy2r (amino acids 1-51) could work as an immunogen for creating antibodies that target the receptor's extracellular domain specifically. The 10xHis tag makes purification and immobilization straightforward for antibody screening assays. Scientists can use this fragment in ELISA-based screening to find antibodies that recognize Npy2r's N-terminal region. Western blot validation with the purified protein might also confirm antibody specificity and help with cross-reactivity testing.
2. Protein-Protein Interaction Studies
The His-tagged N-terminal domain appears useful for pull-down assays aimed at identifying potential binding partners that interact with Npy2r's extracellular region. Since the His tag allows metal affinity purification, researchers can efficiently immobilize it on nickel-based resins for interaction studies. This fragment may prove valuable for studying receptor dimerization or oligomerization through the N-terminal domain. Co-immunoprecipitation experiments could also use this recombinant fragment as bait to capture interacting proteins from cell lysates.
3. Structural and Biochemical Characterization
The recombinant N-terminal fragment provides material for biophysical studies that might reveal structural properties of this specific Npy2r domain. Circular dichroism spectroscopy could help researchers analyze secondary structure content and thermal stability of this receptor region. Mass spectrometry analysis using the purified protein may confirm proper folding and reveal post-translational modifications. Cross-linking experiments might shed light on the spatial organization and conformational changes within the N-terminal domain.
4. Competitive Binding Assays
This N-terminal fragment appears to work as a competitor in binding studies designed to determine whether ligands or other molecules interact with Npy2r's extracellular domain. The fragment could block or compete with full-length receptor binding in cell-based assays. Surface plasmon resonance experiments using this protein may help researchers study binding kinetics with potential ligands or regulatory molecules. The His tag makes immobilization relatively easy for real-time binding analysis and concentration-dependent competition studies.
