Bioactive Recombinant Immune Checkpoint Protein Dimers for Advanced Immunological Applications
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant immune checkpoint proteins, including CD28, CD80, CTLA-4, PD-1, and TIGIT mimic native dimerization to support accurate receptor-ligand interactions and immune signaling studies.
These immune checkpoint receptors are transmembrane proteins that maintain immune homeostasis by balancing activation and inhibition. Dimerization stabilizes ligand interactions and is critical for inhibitory signaling—suppressing autoimmunity and promoting peripheral tolerance. Tumors often exploit these pathways to evade immune surveillance. Mimicking native dimer structures enables mechanistic studies, antibody screening, and development of immunotherapies targeting pathways like PD-1, CTLA-4, and TIGIT.
Conigen’s protein dimers mimic native inhibitory motifs and enable analysis of co-receptor signaling, and the immune checkpoint blockade strategies. Validated in functional binding assays, these reagents are ideal for drug discovery and mechanistic research.
Spotlight: TIGIT
Bioactive Performance
TIGIT is an inhibitory checkpoint receptor that suppresses immune activity in tumors by binding ligands like CD155. Conigen’s bioactive TIGIT protein dimer mimics the native homodimer and shows enhanced binding to its CD155 dimer ligand compared to the monomer.
Human TIGIT protein dimer, Fc-Tag (TIGIT-Fc, CSP-24028) binds to its ligand human CD155 protein dimer (CSP-24029) or monomer as measured by ELISA. CD155 dimer significantly enhances the binding to TIGIT compared to CD155 monomer. CD155 dimer or monomer (0.2 μg/well) was coated on 96-well microtiter plates and detected by serial dilution of TIGIT-Fc.
These recombinant immune checkpoint proteins can be used for drug discovery and basic research, as an immunogen/antigen to generate specific antibodies targeting the natural dimer and study ligand interactions.