Recombinant Influenza A virus Matrix protein 2 (M2) is produced through an in vitro E.coli expression system, covering the complete 1-97 amino acid sequence. The protein comes with an N-terminal 10xHis-tag and a C-terminal Myc-tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows purity levels exceeding 85%. This research-use-only product works well for experimental applications that need high-quality viral proteins.
The Matrix protein 2 (M2) of Influenza A virus appears to play a critical role in the virus's life cycle, especially during viral uncoating and assembly. It works as an ion channel, which seems vital for acidifying the viral interior—a process necessary for genome release. M2 has become a key target in antiviral research and may provide valuable insights into how influenza virus replication and pathogenesis actually work.
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 Characterization
This recombinant M2 protein can work as an immunogen or antigen for creating monoclonal or polyclonal antibodies against influenza A virus M2 protein. The dual His and Myc tags make purification and detection simpler during antibody screening processes. Researchers might use this protein in ELISA-based assays to study antibody binding specificity and affinity. Since the protein covers the full length (1-97aa), antibodies developed against conformational epitopes should be well-represented in the immune response.
2. Protein-Protein Interaction Studies
The N-terminal His tag and C-terminal Myc tag appear suitable for pull-down assays aimed at identifying cellular proteins that interact with influenza A virus M2 protein. Researchers can attach the protein to nickel-affinity resins or anti-Myc antibody-coated beads to capture potential binding partners from cell lysates. These tags also allow for detection and measurement of the protein in co-immunoprecipitation experiments. Studies like these may help clarify the molecular mechanisms behind M2 protein function during viral infection.
3. Biochemical and Structural Analysis
This recombinant M2 protein works in various biochemical assays designed to study its basic properties—protein folding, stability, and how it forms oligomers. The high purity (>85%) makes it appropriate for biophysical characterization techniques like circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation. Researchers can examine how the protein behaves under different pH and salt conditions to better understand its structural characteristics. The dual tags offer convenient ways to detect and measure the protein during these analyses.
4. Vaccine Research and Immunogenicity Studies
This full-length recombinant M2 protein could be valuable in preclinical vaccine development studies to test its immunogenic properties in animal models. Researchers might assess whether the protein can trigger immune responses and compare different adjuvant formulations or delivery approaches. The protein may serve as a reference standard when comparing the immunogenicity of modified M2 variants or fusion proteins. Such studies could contribute to understanding M2 protein's potential as a vaccine component in influenza research.
5. Assay Development and Screening Applications
The dual-tagged M2 protein can help develop and refine various research assays, including sandwich ELISAs, Western blot protocols, and immunofluorescence techniques. The His and Myc tags offer multiple detection options and internal controls for assay validation. Researchers might use this protein to create standard curves for quantitative assays or as a positive control in experimental workflows. The protein could also be useful in screening applications to identify small molecules or compounds that interact with M2 protein for research purposes.
