HLA-G and LILRs

Mammalian-derived HLA-G and their receptors, LILRB/LILRA in various species and tags for first-in-class drug discovery.

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.

Validation Data

We invest considerable time and effort performing quality and activity assays during product development to ensure our proteins are both pure and bioactive.

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).

Custom Products

We offer customization of any of our HLA-G/LILR products or we can work with you to set up an expression system for your novel protein.