HLA-G, like other immune checkpoints, mediates its function by binding to receptors on immune cells.
The known receptors are from the leukocyte Ig-like receptor (LILR) family and include LILRAs (activating) and LILRBs (suppressing).
When HLA-G binds to LILRBs, tumor cells can escape the surveillance of the immune system.
Owing to their role in activation/supression of immune cells, LILR family proteins have shown broad potential for anti-tumor effects.
LILRBs have become hot targets for drug development, especially for discovery of first-in-class drugs.
The HLA-G and ILT-2/4 signaling pathway is a novel target for monoclonal antibody therapy or cell-based immunotherapy.
Figure 1. Human LILRB2, hFc Tag captured on CM5 Chip via Protein A can bind Human HLA-G Tetramer with an affinity constant of 4.62 nM as determined in SPR assay (Biacore T200).
Figure 2. Serial dilutions of Anti-LILRB2 Antibody were added into Human LILRB2, His Tag : Biotinylated HLA-G Complex Tetramer, His Tag binding reactioins. The half maximal inhibitiory concentration (IC50) is 75.3ng/ml.
Figure 3. The purity of Biotinylated Human APOE3 is greater than 95% as determined by SEC-HPLC.
Figure 4. Cynomolgus LILRB2, His Tag immobilized on CM5 Chip can bind Cynomolgus HLA-G Complex Tetramer, His Tag with an affinity constant of 852 nM as determined in SPR assay (Biacore T200).