This recombinant Turnip mosaic virus Polyprotein is expressed in E. coli and comes with an N-terminal 10xHis-tag plus a C-terminal Myc-tag, which makes purification and detection much more straightforward. The protein represents a partial expression covering amino acids 2360-2876. SDS-PAGE analysis shows purity levels above 85%, making it well-suited for research applications that demand high-quality viral protein samples.
The Turnip mosaic virus Polyprotein appears to play a central role in the viral life cycle. It undergoes proteolytic processing that generates multiple functional proteins—these seem necessary for viral replication and assembly. As what may be considered a key viral component, researchers often examine this protein to better understand viral pathogenesis and host-virus interactions. Many also investigate it when developing potential antiviral strategies, hoping to gain insights into the molecular mechanisms behind infection and immunity.
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.
Turnip mosaic virus (TuMV) polyprotein is a complex viral protein that requires precise folding, proper post-translational processing by viral proteases, and specific tertiary structure for its functional activity in viral replication and infection. The E. coli expression system cannot provide the eukaryotic folding environment or viral protease activity required for proper polyprotein processing and maturation. The partial fragment (2360-2876aa) represents only a small portion of the full polyprotein and lacks the complete structural context. The dual N-terminal 10xHis-tag and C-terminal Myc-tag are large relative to the fragment size and may cause significant steric interference. The probability of correct folding with functional viral activity is extremely low.
1. Antibody Development and Characterization
This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional protein folding. The defined fragment provides specific epitopes within the 2360-2876aa region for generating TuMV-specific antibodies. The high purity (>85%) ensures minimal contamination-related issues during immunization.
2. Protein Structure-Function Analysis
Basic biophysical characterization can be performed, but will not reflect native viral protein structure. The lack of proper processing and the presence of large tags mean results will describe an artificial fragment rather than the authentic viral protein. The tags will dominate the protein's physical properties.
3. ELISA Development
This application is well-suited for developing detection assays. The protein serves as an excellent standard for ELISA development, as immunoassays depend on epitope recognition rather than functional conformation. The dual tags provide flexible detection options.
Final Recommendation & Action Plan
This partial TuMV polyprotein fragment with dual tags is unsuitable for functional viral studies due to the essential requirements for polyprotein processing and eukaryotic folding that cannot be met in this expression system. The protein should not be used for interaction studies and viral polyprotein processing studies. Applications 1 and 3 (antibody development and ELISA) can proceed immediately. Application 2 provides only basic physical characterization of the fragment. For reliable TuMV research requiring native functionality, use full-length polyprotein expressed in plant or eukaryotic systems that support proper processing and maturation.
