SPR Binding Assay Service

Surface plasmon resonance (SPR) is a cornerstone technology at CD BioSciences for real-time, label-free analysis of biomolecular interactions. Our expert SPR Binding Assay service delivers precise kinetic and affinity data, providing critical insights for epigenetic mechanism exploration and drug discovery. We empower researchers with reliable data to characterize interactions with confidence and accelerate their research progress.

Overview of Surface Plasmon Resonance (SPR)

SPR is a powerful label-free technique, widely recognized as the gold standard for real-time analysis of biomolecular interactions. Its working principle relies on detecting changes in the refractive index on the sensor chip surface to monitor in real time the binding process between an analyte and an immobilized ligand, producing sensorgrams that reflect binding details. This technology not only provides affinity data but also yields key kinetic parameters, namely the association rate constant (ka) and the dissociation rate constant (kd). This enables in-depth insights into binding mechanisms, characterization of inhibitor properties.

Fig.1 The mechanism of surface plasmon resonance (SPR). (Murali S, et al., 2022)

In epigenetic research, SPR is pivotal for studying interactions such as:

1. Binding of histone-modifying enzymes (e.g., HDACs, HATs) with their inhibitors or activators.
2. Validation of transcription factor binding to specific DNA sequences.
3. Analysis of protein-protein complex formation within epigenetic complexes.

Our Services

Building on our advanced SPR platforms, we offer a comprehensive suite of binding assays tailored to diverse research needs. Our services encompass detailed kinetic profiling, competition studies, and epitope mapping. Supported by rigorous quality control, we ensure the delivery of high-quality, reproducible data to support your most demanding interaction analysis projects.

We offer comprehensive SPR analysis tailored to your research objectives:

1. Kinetic and Affinity Analysis: Precise determination of association rate (ka), dissociation rate (kd), and equilibrium dissociation constant (KD).
2. Competition/Inhibition Assays: Evaluate if a candidate molecule competitively inhibits the interaction between a known ligand and its target.
3. Epitope Mapping: Identify the specific binding region of an antibody or protein on its target molecule.
4. Concentration Analysis: Accurately determine the active concentration of an analyte in solution.
5. Interaction Types: We analyze Protein-Protein, Protein-DNA/RNA, Protein-Small Molecule, and Antibody-Antigen interactions.

Service Workflow

Sample Requirements

1. Ligand (for immobilization): High purity (>90%), recommended concentration, buffer details.
2. Analyte: Molecular weight, required purity (>95%), buffer composition.
3. Minimum sample volumes will be specified upon project design.

Deliverables

Upon completion, you will receive:

1. A detailed final report including all experimental parameters.
2. All original sensorgram data and fitted curves.
3. Calculated kinetic and affinity constants (ka, kd, KD).
4. Professional interpretation and conclusions.

CD BioSciences' Technology Advantages

Our services are powered by state-of-the-art SPR platforms (e.g., Biacore series) ensuring high-quality, reproducible data. Our key advantages lie in:

1. Label-Free Detection: No need for fluorescent or radioactive tags, preserving molecular native state.
2. Real-Time Monitoring: Observe binding events directly for a full kinetic profile.
3. High Sensitivity & Low Sample Consumption.
4. Quantitative Rigor: Provides robust kinetic and affinity constants.

Frequently Asked Questions (FAQs)

Ready to characterize your biomolecular interactions with precision? Contact us today for a free project consultation and a detailed quote. We are here to support your research every step of the way.

Reference

1. Murali S, Rustandi R R, Zheng X, et al. Applications of surface plasmon resonance and biolayer interferometry for virus–ligand binding[J]. Viruses, 2022, 14(4): 717.