Recombinant Mouse Anthrax toxin receptor 1 (Antxr1) is 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.
Mouse Anthrax toxin receptor 1 (Antxr1) is a transmembrane receptor that requires precise folding, proper domain organization, and specific tertiary structure for its functional activity in toxin binding and cellular signaling. The mammalian cell expression system provides the eukaryotic folding environment necessary for correct disulfide bond formation and post-translational modifications. However, the partial fragment (31-319aa) lacks critical domains, including the transmembrane region and cytoplasmic tail, essential for full receptor functionality. The dual N-terminal 6xHis-Myc tag may cause some steric interference with the protein's functional domains. While the mammalian expression favors proper folding, the probability of correct folding with functional receptor activity requires experimental validation due to the truncated nature of the construct.
1. Protein-Protein Interaction Studies
This application carries a moderate risk without functional validation. Antxr1 interactions with ligands (e.g., anthrax toxin) require precise tertiary structure and proper domain conformation. If correctly folded and active (verified through binding assays), the protein may identify physiological interaction partners. If misfolded/unverified, there is a risk of non-specific binding or failure to replicate genuine receptor-ligand interactions.
2. Antibody Development and Validation
This application is highly suitable as antibody development relies on antigenic sequence recognition. The mammalian-expressed protein provides proper folding and relevant post-translational modifications, making it an excellent immunogen for generating antibodies that recognize native Antxr1 epitopes.
3. Structural and Biochemical Characterization
These studies are essential for determining folding status. The mammalian expression system supports proper folding, making techniques like circular dichroism spectroscopy and dynamic light scattering valuable for assessing the extracellular domain's structural properties.
4. Cell-Based Binding and Uptake Assays
This application carries significant limitations. While the soluble extracellular domain can be used for binding studies, it lacks the transmembrane domain required for physiological receptor function. Binding data may not reflect native receptor behavior, and uptake studies are fundamentally impossible without full-length receptor expression.
Final Recommendation & Action Plan
The mammalian-expressed Antxr1 extracellular domain fragment has a high probability of correct folding due to the appropriate expression system, but its functional applications are limited by the lack of transmembrane and cytoplasmic domains. Begin with Application 3 (Structural Characterization) to validate folding quality. Application 2 (antibody development) can proceed immediately. Applications 1 and 4 require rigorous validation of binding functionality before use, recognizing that the soluble fragment cannot replicate full receptor function. For complete Antxr1 studies, use a full-length protein expressed in mammalian systems with proper membrane integration.
