Recombinant Murine polyomavirus Major capsid protein VP1 is expressed in E. coli, covering the full length of the mature protein from amino acids 2 to 373. A C-terminal 6xHis tag is included to help with purification and detection. The protein reaches greater than 85% purity, as confirmed by SDS-PAGE, and works well for research applications. This product is designed for in vitro studies and maintains low endotoxin levels.
The Major capsid protein VP1 appears to be essential for viral capsid assembly in Murine polyomavirus. It likely plays a crucial role in protecting the viral genome, maintaining virus stability, and helping the virus interact with host cells. As a key structural component, VP1 proves valuable for studying viral assembly and pathogenesis, which makes it an important target in virology research.
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. Viral Capsid Assembly and Structure Studies
This recombinant VP1 protein can help investigate how murine polyomavirus capsids self-assemble in vitro. The full-length mature protein (2-373aa) retains all the structural domains needed for capsid formation. This makes it well-suited for electron microscopy studies and dynamic light scattering experiments. Researchers can explore what conditions are needed for VP1 pentamer formation and more complex capsid assembly. The C-terminal His-tag helps with purification and immobilization for structural analysis techniques.
2. Antibody Development and Immunological Studies
The recombinant VP1 protein works well as an antigen for creating polyclonal and monoclonal antibodies specific to murine polyomavirus. E. coli expression produces enough protein for immunization protocols and follow-up antibody screening assays. The His-tag allows efficient purification for ELISA-based antibody characterization and epitope mapping studies. These antibodies can then be used in various research applications, including viral detection assays and capsid protein localization studies.
3. Protein-Protein Interaction Studies
The His-tagged VP1 protein works in pull-down assays to identify cellular proteins that interact with the viral capsid during infection. The tag allows immobilization on nickel-affinity matrices, which enables co-precipitation of binding partners from cell lysates. This approach may help reveal host-virus interactions and identify cellular receptors or co-factors involved in viral entry mechanisms. The full-length protein ensures that all potential interaction domains remain intact for comprehensive binding studies.
4. Biochemical Characterization and Functional Analysis
This recombinant protein provides a platform for detailed biochemical analysis of VP1 properties. These include thermal stability, pH sensitivity, and proteolytic susceptibility. Researchers can perform comparative studies between different polyomavirus VP1 proteins to understand species-specific differences in capsid stability and behavior. The purified protein can also help establish baseline biochemical parameters for the murine polyomavirus capsid protein under controlled in vitro conditions.
