Surface Plasmon Resonance technology, developed in the 1990s, is a novel technique that employs the principles of SPR to detect the interactions between ligands and analytes on biosensor chips. By real-time analysis, it allows for the simple and rapid monitoring of interactions between various biomolecules such as DNA and proteins, proteins and proteins, drugs and proteins, nucleic acids and nucleic acids, antigens and antibodies, receptors and ligands, etc. This technology finds widespread applications in life science research, drug screening, food testing, environmental monitoring, and other fields.

（Drescher DG, et al. Adv Protein Chem Struct Biol. 2018）

When light travels from an optically dense medium to an optically sparse medium, total internal reflection occurs under specific conditions. In a surface plasmon resonance instrument, the core structure is the SPR chip (a metal surface with dextran that allows ligand proteins to be immobilized by binding to the dextran). A crucial step in SPR analysis is immobilizing ligands (depicted as partially circular shapes) on the surface of the biosensor chip. This allows analyte proteins to move through the flow channel, binding to the immobilized ligands on the sensor surface, leading to changes in the surface refractive index and a shift in the reflected 'resonance shadow' from 1 to 2. The intensity changes with the variation in angle/shadow angle, depicted graphically in the upper right corner of the illustration from angle 1 to angle 2. The resonance signal/dip, showing the movement over time, is displayed in the sensorgram below. This overall image corresponds to the real-time detection by the detector of the binding and dissociation of molecules in the flow channel solution with molecules on the chip surface, presented in the form of SPR response values.

⭕ Real-time detection, capable of dynamically monitoring the entire process of biomolecular interactions

⭕ No need for labeled samples, preserving molecular activity

⭕ Requires minimal sample amounts, typically 100 μg of protein per surface

⭕ Convenient and fast detection process with high sensitivity

⭕ Widely applicable in various fields

⭕ High-throughput, high-quality analytical data

⭕ Ability to track and monitor the stability of immobilized ligands

The sample injection method can adopt either a single-cycle or a multi-cycle mode. Depending on the molecular interaction mechanism, the results analysis can use either kinetic or steady-state affinity analysis mode.

（Injection modes: Left - Multi-cycle, Right - Single-cycle）

（Results analysis: Left - Kinetic analysis, Right - Steady-state analysis）

》Detection of interactions between biomolecules (proteins, small molecules, antibodies)

》Inhibitor screening

 》Antibody screening

We have developed a screening platform based on existing recombinant proteins and single B cell-derived recombinant rabbit monoclonal antibodies. The core members of our technical team have extensive experience in protein research, biomolecular interaction analysis, and protein characterization studies. Our company has established a rigorous process for method development and optimization, and we are ISO9001 certified, ensuring optimal results for each detection experiment. Currently, we offer services for affinity testing, including protein interactions and antibody screening.