Bioactive Recombinant Tumor-Associated Antigen Proteins for Advanced Cancer Research
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant tumor-associated antigens (TAAs), including HER2, Trop-2, and Nectin-4 mimic native quaternary conformations that are essential for understanding cancer progression and advancing targeted therapies. Many TAAs dimerize to drive oncogenic signaling or modulate immune recognition.
TAAs are aberrantly expressed proteins that serve as biomarkers and therapeutic targets in cancer. Dimerization stabilizes receptor-ligand interactions and enhances signaling, shaping the development of monoclonal antibodies, CAR-T therapies, and bispecifics. Conigen’s recombinant protein dimers mimic these native conformations, enabling high-sensitivity screening and epitope-specific discovery.
Spotlight: Nectin-4
Bioactive Performance
Nectin-4 is a tumor-associated antigen involved in cell adhesion and immune modulation. Conigen’s Nectin-4 protein dimer mimics its native dimer configuration and shows enhanced binding to the TIGIT protein dimer compared to monomeric forms.
Human Nectin-4 protein dimer, His-Tag (CSP-24016) or Nectin-4 protein monomer binding to TIGIT protein dimer, Fc-Tag (TIGIT-Fc, CSP-24028) as measured by ELISA. Nectin-4 protein dimer significantly enhances the binding to TIGIT compared to Nectin-4 monomer. The Nectin-4 protein dimer or monomer (0.2 μg/ml) was coated on 96-well microtiter plates and detected by serial dilutions of TIGIT-Fc.
These recombinant proteins are ideal for studying receptor-ligand dynamics, therapeutic antibody development, and cancer biology research.