This recombinant Human herpesvirus 8 type P Viral macrophage inflammatory protein 2 (VMI2) comes from E. coli expression and covers the 24-93 amino acid region. It's provided tag-free for research applications. SDS-PAGE analysis confirms the protein reaches purity levels above 97%. The protein maintains full biological activity, which appears evident through its inhibitory effect on monocyte migration when exposed to human MIP-1 alpha. LAL method testing keeps endotoxin levels below 1.0 EU/µg.
Viral macrophage inflammatory protein 2 (VMI2) from Human herpesvirus 8 seems to play a central role in shaping immune responses by disrupting chemokine signaling pathways. Its capacity to block monocyte migration may be crucial for understanding how viruses evade immune detection. The way VMI2 interacts with chemokines makes it a compelling research target in viral pathogenesis and immunological studies focused on Kaposi's sarcoma-associated herpesvirus.
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. Monocyte Migration Inhibition Assays
This application is well-supported. The protein has confirmed biological activity in inhibiting monocyte migration response to human VMI2 at concentrations of 1.0-10.0 μg/ml. The high purity (>97%) and low endotoxin levels (<1.0 EU/μg) make it suitable for cell-based assays without triggering non-specific inflammatory responses. This recombinant protein can be reliably used to study chemokine antagonism mechanisms.
2. Chemokine Receptor Binding Competition Studies
This application is appropriate given the confirmed bioactivity. The protein's ability to inhibit VMI2-induced migration strongly suggests receptor interaction capabilities. The high purity supports quantitative binding studies to determine IC50 values and binding kinetics. However, it should be noted that while the functional activity implies receptor binding, direct binding studies would need to be validated experimentally.
3. Antibody Development and Immunoassay Applications
This application is well-supported. The high purity (>97%), low endotoxin levels, and confirmed bioactivity make this an excellent immunogen for antibody production. The partial sequence (24-93aa) represents a defined antigenic region. The tag-free nature avoids potential immune responses to tags, making it suitable for generating antibodies specific to the viral protein.
4. Viral Pathogenesis Research Models
This application is appropriate. The confirmed biological activity and high purity make this protein suitable for studying HHV-8 immune evasion mechanisms. The demonstrated inhibitory effect on monocyte migration provides a solid foundation for pathogenesis studies examining how viral chemokines alter host immune responses.
Final Recommendation & Action Plan
This recombinant viral MIP-2 protein is highly suitable for all described applications due to its confirmed biological activity, high purity (>97%), and low endotoxin levels. The protein has been validated against a standard and shows specific inhibitory activity on monocyte migration. Researchers can proceed confidently with monocyte migration assays, receptor binding studies, antibody development, and pathogenesis research without needing additional folding validation. For optimal results, follow the specified concentration ranges (1.0-10.0 μg/ml) established in the activity validation, and include appropriate controls (e.g., VMI2 alone) in migration experiments. The E. coli expression system successfully produced a functional chemokine analog despite being a prokaryotic system, likely because this viral protein is relatively small and may not require complex eukaryotic post-translational modifications for activity.
