Recombinant Vaccinia virus Protein K3 (VACWR034) is manufactured using a yeast expression system. The protein spans the complete sequence from amino acids 1 to 88. An N-terminal 6xHis-tag is attached, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the purity exceeds 90%. This product is intended strictly for research purposes and appears to deliver consistent results across different experimental conditions.
Protein K3 from vaccinia virus seems to play a key role in how the virus manipulates host immune responses. The protein likely participates in pathways that disrupt the host's natural antiviral defenses, which is why it has become an important focus in virology and immunology studies. Learning more about how K3 functions may provide valuable insights into viral disease mechanisms and the complex interactions between pathogens and their hosts - knowledge that could prove essential for creating new treatments.
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. Vaccinia Virus Protein Interaction Studies
This recombinant K3 protein works well as either bait or target in pull-down experiments designed to find host cell proteins that interact with vaccinia virus during infection. The N-terminal 6xHis tag allows for straightforward attachment to nickel-affinity resins, making co-immunoprecipitation experiments with host cell lysates relatively simple. These types of studies might help researchers better understand the specific molecular processes that vaccinia virus uses to alter host cell behavior throughout its life cycle.
2. Antibody Development and Characterization
Researchers can use the purified K3 protein as an immunogen to create polyclonal or monoclonal antibodies that specifically recognize this vaccinia virus protein. The high purity level (over 90%) means there's minimal contamination that might cause unwanted cross-reactions with other proteins. Scientists would find these antibodies quite useful for investigating K3 protein expression patterns, cellular location, and biological function in vaccinia-infected cells using methods like Western blotting, immunofluorescence microscopy, and flow cytometry.
3. Biochemical and Biophysical Characterization
This recombinant protein offers a good starting point for in-depth biochemical studies of K3's inherent properties. Researchers can examine factors like heat stability, how the protein responds to different pH levels, and its overall structural features. Methods such as circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation may help scientists understand how the protein folds, whether it forms complexes with itself, and how its shape changes under different conditions. The yeast expression system combined with His-tag purification should produce properly folded protein that's suitable for these types of detailed analyses.
4. Enzyme-Linked Immunosorbent Assays (ELISA)
The His-tagged K3 protein attaches easily to ELISA plates, making it possible to develop precise immunoassays for detecting anti-K3 antibodies in experimental samples. This approach proves particularly valuable when monitoring immune responses in laboratory animals exposed to vaccinia virus or when screening hybridoma cell culture supernatants during antibody production projects. The protein's high purity helps ensure that assays produce reliable, repeatable results with little background noise that could interfere with accurate measurements.
