Recombinant Anas platyrhynchos Lysozyme C-1 is produced using an E. coli expression system and includes a full-length mature protein spanning amino acids 19-147. The protein comes with an N-terminal 6xHis-SUMO tag to make purification and detection easier. SDS-PAGE analysis shows it reaches greater than 90% purity. This product is meant for research use only and appears to offer consistent quality for various experimental applications.
Lysozyme C-1 likely plays a crucial role in how Anas platyrhynchos defends itself by showing antibacterial activity. The protein works by breaking down the peptidoglycan layer of bacterial cell walls - something that's essential for keeping cell wall integrity intact. This makes it valuable for research focused on innate immunity and microbial interactions, potentially offering insights into how immune systems evolved across different species.
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. Comparative Lysozyme Structure-Function Studies
This recombinant mallard lysozyme C-1 could serve as a useful tool for comparative studies looking at lysozyme evolution and how structures differ between species. The N-terminal His-SUMO tag makes purification straightforward and allows for immobilization during biochemical characterization experiments. Scientists can compare this avian lysozyme with versions from mammals and other bird species to better understand evolutionary adaptations. With >90% purity, it seems well-suited for detailed biochemical analysis and comparative enzyme kinetics studies.
2. Antibody Development and Immunological Research
The recombinant protein may work as an immunogen for creating specific antibodies against mallard lysozyme C-1, or it could function as a standard in immunoassays. The His-SUMO tag helps with purification and can be used in tag-based detection systems - though it can also be removed if researchers need the native protein. This application appears particularly valuable for wildlife immunology research and developing tools to study lysozyme expression in waterfowl species. The high purity level suggests minimal cross-reactivity with other proteins during antibody production.
3. Protein-Protein Interaction Studies
Researchers can use the His-tagged lysozyme in pull-down assays to identify potential binding partners or substrates from mallard tissue extracts or other biological samples. The SUMO tag might also help with protein folding and stability during interaction studies. Scientists could investigate lysozyme's role beyond antimicrobial activity - perhaps looking at interactions with other immune system components. The tag system makes immobilization on affinity matrices relatively simple for systematic interaction screening.
4. Biochemical Characterization and Enzyme Assays
Even though biological activity testing hasn't been confirmed, this recombinant lysozyme could help establish and optimize activity assays specific for mallard lysozyme C-1. Researchers might test various substrates and conditions to characterize the enzyme's biochemical properties, including pH and temperature optima. The protein could serve as a reference standard for developing lysozyme activity assays in avian research. The high purity level suggests it would give reliable and reproducible results in biochemical characterization experiments.
