Recombinant Human Butyrophilin subfamily 3 member A1 (BTN3A1) is expressed in a yeast system, spanning amino acids 30-254. This partial protein includes an N-terminal 6xHis-tag for simplified purification and detection. The product achieves a purity of over 90%, as confirmed by SDS-PAGE analysis, which appears suitable for research applications requiring high purity.
BTN3A1 is a protein that seems to modulate immune responses. Part of the butyrophilin family, it likely plays a role in cellular signaling pathways. Research suggests BTN3A1 interacts with immune cells, indicating its potential importance in studies of immune system regulation.
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 Studies
This recombinant BTN3A1 protein fragment (30-254aa) may serve as an immunogen or antigen for developing monoclonal or polyclonal antibodies targeting human BTN3A1. The N-terminal 6xHis tag allows for straightforward purification and immobilization during antibody screening assays. High purity levels (>90%) suggest reliable epitope presentation for antibody binding studies and specificity validation. ELISA-based assays could potentially characterize antibody binding kinetics and cross-reactivity profiles using this protein.
2. Protein-Protein Interaction Studies
Pull-down assays might benefit from the 6xHis-tagged BTN3A1 fragment to identify and characterize potential binding partners or interacting proteins. The tag allows immobilization on nickel-affinity matrices, which could capture interacting molecules from cell lysates or purified protein libraries. This approach appears particularly valuable for mapping interaction domains within the 30-254aa region and understanding BTN3A1's molecular partnerships in cellular environments.
3. Structural and Biochemical Characterization
This purified BTN3A1 protein fragment provides material for biophysical studies. These might include circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation to examine folding properties and oligomerization state. The defined amino acid boundaries (30-254aa) make it appropriate for domain-specific structural analysis and stability studies. The yeast expression system and high purity level likely ensure adequate protein quality for detailed biochemical characterization experiments.
4. Cell-Based Binding and Localization Studies
Researchers could potentially use the recombinant BTN3A1 fragment as an external probe in cell-based assays to study receptor binding or cell surface interactions. Fluorescent labeling or biotinylation of the protein may enable flow cytometry analysis or microscopy-based localization studies. This application allows investigation of BTN3A1's interaction with cell surface receptors or its binding specificity across different cell types under controlled experimental conditions.
