While the recombinant protein itself is non-functional in isolation, its study informs CD9’s roles in:
Sperm-egg fusion: CD9 interacts with integrins (e.g., α6β1) and sperm ADAM proteins to facilitate fertilization .
Viral modulation: CD9 inhibits HIV-1-induced syncytia formation by arresting hemifusion , though its role in Chlorocebus aethiops systems remains unexplored.
Immune regulation: Associates with MHC-II and integrins in dendritic cells to regulate antigen presentation .
The recombinant Chlorocebus aethiops CD9 is produced via bacterial expression, with stringent quality assurance:
| Parameter | Detail |
|---|---|
| Expression Host | E. coli (plasmid-based) |
| Expression Conditions | Optimized for solubility and proper folding |
| Purification Method | Affinity chromatography (His tag) |
| Contaminant Testing | Validated via SDS-PAGE (5% stacking, 15% resolving gel) |
| Stability | Lyophilized powder; avoid repeated freeze-thaw cycles |
Key differences between Chlorocebus aethiops and human CD9 recombinant proteins include:
| Feature | Chlorocebus aethiops CD9 | Human CD9 |
|---|---|---|
| Host System | E. coli | Wheat germ, mammalian cells |
| Tag | His | His, GST, Fc-Avi |
| Protein Length | Full-length (2–228 aa) | Fragment (112–195 aa, wheat germ) |
| Applications | Structural studies, viral research | ELISA, WB, SDS-PAGE |
| Purity | >90% (SDS-PAGE) | >95% (HPLC, SEC) |
This recombinant protein serves as a tool for:
Structural studies: Mapping TM domains and extracellular loops critical for tetraspanin interactions .
Viral entry mechanisms: Investigating CD9’s role in modulating viral fusion (e.g., morbilliviruses) .
Therapeutic target validation: Screening CD9 inhibitors for cancer or inflammatory diseases .
Functional limitations: Lacks post-translational modifications (e.g., glycosylation) due to bacterial expression .
Handling requirements: Lyophilized aliquots must be stored at -20°C/-80°C to prevent degradation .
Species specificity: Results may not directly translate to human systems due to evolutionary divergence in tetraspanin domains .