BPS Bioscience的蛋白质结合研究服务 / BLI 检测服务

BPS Bioscience offers Bio-Layer Interferometry (BLI) services to evaluate and analyze protein interactions. Label free analysis is a critical research method to determine the binding kinetic parameters of compounds. These studies are of key importance for pharmaceutical and biotechnological preclinical drug development. Utilize BPS Biosciences’ BLI services for deeper insight into your protein studies through measuring binding kinetics, steady state affinity, and through target validation. BPS will provide accurate and sensitive kinetic studies in a timely manner to further progress your research.

Services offered include

• Protein immobilization

• Binding affinity measurements of experimental points

• Data fitting and reporting

• Access to BPS Bioscience’s extensive protein portfolio for target proteins

• A final report outlining all data, methods, and results

Contact us for more information about our BLI services and to learn more about how BPS Bioscience can further progress your research.

Figure 1: BLI binding analysis of human anti-ACE2 antibody to immobilized ACE2-His (BPS Bioscience #11003) via anti-His probes. KD = 144 nM.

Figure 2: BLI binding analysis of SARS-CoV-2 Spike (RBD) to immobilized ACE2-His (BPS Bioscience #11003) via anti-His probes. KD = 1.2 nM.

Figure 3:PD-1-His Immobilization
Loading: PD-1-His immobilization: PD-1-His (BPS Bioscience #71198) titration from 400 to 6.25 nM, 2-fold serial dilution.
Results: Anti-His probes are able to immobilize PD-1-His in the nM range.

Figure 4: PD-1-His:PD-L1 binding, Loading: 100 nM PD-1-His (BPS Bioscience #71198)
Association/disassociation: PD-L1 (BPS Bioscience #71104) titration from 400 to 6.25 nM, 2-fold serial dilution
Results: PD-L1 binds to immobilized PD-1 with high affinity.
koff = 5.21 ± 1.03 x 10-4 s-1: kon = 7.44 ± 0.05 x 10-5 M-1 s-1
KD = 0.7 nM

Figure 5 and Figure 6: PD-1-His:Anti-PD-1 binding
Loading: 100 nM PD-1-His (#71198)
Association/disassociation: Anti-PD-1 (BPS Bioscience #71120) titration from 100 to 3.125 nM, 2-fold serial dilution
Results: Anti-PD-1 binds to immobilized PD-1 with high affinity. Very slow disassociation, unable to obtain accurate koff. Steady-state data: KD = 7.2 ± 0.5 nM

Figure 7: PD-1-His:PD-L1 vs Anti-PD-L1 competition
Loading: 100 nM PD-1-His (BPS Bioscience #71198)
Association/disassociation: competition between 100 nM PD-L1 (BPS Bioscience #71104) and Anti-PD-L1 (BPS Bioscience #71213) titration from 100 to 0.3 nM, 4-fold serial dilution
Anti-PD-L1 sequesters PD-L1 in a concentration-dependent manner, reducing binding of PD-L1 to PD-1. IC50 in the range of decens of nM (green trace = 25 nM Anti-PD-L1, approximately 50% binding reduction).