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.
Anas platyrhynchos Lysozyme C-1 is a eukaryotic enzyme that requires precise disulfide bond formation and proper tertiary structure for its muramidase activity. The E. coli expression system cannot perform the necessary post-translational modifications (particularly proper disulfide bonding) that are critical for this enzyme's native conformation. The large N-terminal SUMO tag (∼15 kDa) may sterically interfere with the active site or proper folding. While the protein may be soluble, it is highly unlikely to achieve the correct folding needed for functional lysozyme activity. The probability of correct folding with enzymatic function is low.
1. Comparative Lysozyme Structure-Function Studies
This application is suitable for sequence-based comparisons and immunological cross-reactivity studies but not for functional comparative analyses. Functional comparative studies require properly folded, active enzymes that this misfolded variant cannot provide. A misfolded lysozyme will not provide meaningful data on enzymatic activity differences between species. Structural comparisons should be limited to sequence alignment and epitope mapping rather than functional enzymology.
2. Antibody Development and Immunological Research
This recombinant lysozyme serves as an excellent immunogen for generating antibodies against linear epitopes of duck lysozyme C-1. The full-length mature sequence ensures comprehensive epitope coverage. The SUMO tag facilitates purification and immunization procedures. However, antibodies may not efficiently recognize conformational epitopes on the native, properly folded enzyme.
3. Biochemical Characterization and Enzyme Assays
This is the essential first step to assess physical properties but not for functional enzyme assays. Techniques like circular dichroism can analyze secondary structure content, while thermal shift assays evaluate stability. However, enzymatic activity assays will likely yield negative results due to probable misfolding and are not recommended without activity validation.
Final Recommendation & Action Plan
This recombinant lysozyme is primarily suitable for antibody development and biophysical characterization but fundamentally unsuitable for functional studies due to E. coli's inability to produce properly folded eukaryotic enzyme. The immediate priority is Application 3 (Biochemical Characterization) to assess the protein's physical properties through CD spectroscopy and SEC analysis. Application 2 (Antibody Development) can proceed immediately. Application 1 should be limited to non-functional comparative studies. For functional lysozyme studies, alternative approaches using eukaryotic expression systems or native purification from duck eggs are essential.
