Recombinant Mouse Anthrax toxin receptor 1 (Antxr1) gets expressed in a mammalian cell system, which should help with proper folding and post-translational modifications. This partial protein covers amino acids 31-319 and comes with an N-terminal 6xHis-Myc tag for easier purification and detection. The product shows purity levels above 90% when tested by SDS-PAGE. This makes it a dependable option for research that needs high-quality protein samples.
Anthrax toxin receptor 1 (Antxr1) plays a key role in cellular processes as a receptor for anthrax toxin. It helps mediate toxin entry into cells. The receptor is also part of the larger cell surface receptor signaling network. Because of these functions, Antxr1 has become an important research target for understanding how receptors and ligands interact, and how cells respond in different experimental settings.
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. Protein-Protein Interaction Studies
This recombinant mouse Antxr1 protein works well for investigating binding interactions with potential ligands or other proteins in laboratory conditions. The N-terminal 6xHis-Myc tag makes it straightforward to attach the protein to nickel-affinity surfaces for surface plasmon resonance (SPR) or bio-layer interferometry (BLI) experiments. Pull-down assays that take advantage of the His-tag may help identify new binding partners from mouse cell lysates or tissue extracts. The high purity (>90%) appears to support reliable binding kinetics measurements while reducing unwanted interactions in biochemical assays.
2. Antibody Development and Validation
The recombinant protein works as an effective immunogen or screening antigen for creating mouse Antxr1-specific antibodies. Since it's expressed in mammalian cells, the protein likely maintains proper folding and post-translational modifications that mirror the native mouse protein. The Myc tag offers an internal control for protein detection and can help validate antibody specificity through competitive binding assays. Researchers can also apply this protein in ELISA-based screening of hybridoma supernatants or phage display libraries that target mouse Antxr1.
3. Structural and Biochemical Characterization
The purified recombinant protein can undergo biophysical analysis to determine its structural properties and stability. Methods like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation may provide insights into protein folding, oligomerization state, and thermal stability. The defined expression region (31-319aa) represents a specific domain or shortened form that researchers can compare to full-length protein in structural studies. Mass spectrometry analysis can confirm the expected molecular weight and identify any post-translational modifications that occur during mammalian cell expression.
4. Cell-Based Binding and Uptake Assays
The His-Myc tagged protein works in cell culture experiments to study receptor-mediated binding and internalization processes. Fluorescently labeled or biotinylated versions of this protein can be created through tag-specific conjugation methods for flow cytometry or microscopy-based cellular uptake studies. The protein serves as a tool to investigate competitive binding with natural ligands in mouse cell lines that express Antxr1. Time-course experiments might reveal binding kinetics and cellular trafficking patterns in relevant mouse cell models.
