Affinity Measurement Services for Various Ligands and Analytes

Scientists from Creative Biolabs have extensive experience in affinity and kinetics measurements of biomolecular interactions. We are capable of satisfying any specific demand from our customer.

Affinity and kinetics measurements of biomolecular interactions is a hot issue that researchers concern in recent decades. To perform this, a wide range of methods can be used, such as micro Kjeldahl determinations for protein, Maxam-Gilbert for nucleic acids, and other specific methods for measuring particular biomolecule.

Both Surface Plasmon Resonance (SPR) and Bio-Layer Interferometry (BLI) technologies use a label-free approach to monitor biomolecular interactions as well as providing informations of kinetics and specificity of binding in real time. The platforms based on SPR and BLI technologies (Biacore, ProteOn and Octet) employs the binding of various concentrations of analyte to the immobilized ligands (Figure 1). Based on Biacore, ProteOn and Octet systems, we can provide pharmaceutical development, quality control of biomolecular interactions

Figure 1. The principle of SPR (left panel) and BLI (right panel) technologies.Figure 1. The principle of SPR (left panel) and BLI (right panel) technologies.

For various ligands and analytes interactions, we can provide the in-depth analyses as below:

Figure 2. The calculation of KD value.Figure 2. The calculation of KD value.

Both SPR and BLI technologies are simplified and high-throughput assay approaches, which are the most suitable for analyte concentration and affinity measurements.


  1. Biacore Assay Handbook. 29-0194-00 Edition AA, GE Healthcare. F. Markey (1999). Measuring concentration why BIACORE is best. Methodology. 2: 8-11. Protein Interaction Analysis. Bulletin 6044, Bio-rad.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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