Protein Interaction Testings
Biologics Affinity & Kinetic Characterization

Biologics Affinity & Kinetic Characterization

Here at Interactome, Inc. we use the SPR and BLI technologies to analyze biospecific interactions of protein-protein/protein-small molecules. We are specializing in biospecific interactions analysis and the application of SPR/BLI technology for for our customers from the pharmaceutical, biotechnological and diagnostic industry. Our team has acquired long experience and expert knowledge in the application of biosensors based on SPR and BLI. We have a number of modern SPR/BLI sensors suitable for various applications available in our lab ensuring a fast analysis tailored to your special needs. 

Octet BLI vs Biacore SPR



Detection Technology

Bio-Layer Interferometry (BLI)

Surface Plasmon Resonance (SPR)

Signal Read Out

Wave Length Shift

Refractive Index

High Throughput

Yes – 96-well plate format allowing for

multiple samples in a single run

No-  4 channel set-up. Limits the number of samples per run

Sample Recovery

Ability to fully recover samples for use in additional assays

Limited sample recovery as samples are consumed for analysis

Sample Analysis Time

As short as 24 minutes for 96 samples

Typically 3-4 hours for 3 samples

Costs per sample

Cost Effective

Relatively High



Equilibrium dissociation constant. Can be obtained by kinetic or classical equilibrium binding analysis. Provides information about the strength but not the dynamics of an interaction.


Binding enthalpy. KD values at different temperatures can be used to obtain the binding enthalpy of an interaction via vant-Hoff-plots.



ka (kon)
Association rate constant. Provides information on how fast complexes form; can be used for KD determination.


kd (koff)

Dissociation rate constant. Provides information on how fast complexes dissociate; can be used for KD determination.


Equilibrium dissociation constant. Can be obtained by kinetic or classical equilibrium binding analysis. Provides information about the strength but not the dynamics of an interaction.

High lights

No flluidics

– sensor tips (no chips)
– micro-well plates
– easy sample recovery



– no fluorescent dyes required
– numerous coupling methods
– covalent and affinity-based



– Free choice of assay buffers
– Gylcerol and DMSO
– Crude biofluids


Dynamic range

Detectable affinities from pM to mM

Sample requirements

Ligand: The ligand should be homogeneous and more than 90% pure when used for covalent binding to the sensor chip. For one immobilization of a molecule using amine coupling, 1-10 µg is normally sufficient.

The properties of the ligand, which when known are helpful in experiments, are the molecular mass, iso-electric point and the number of lysine's.

Analyte: The analyte concentration of stock solutions should be between 0.1 - 1 mg/ml and free of particles and compounds with large refractive index (e.g. glycerol). The amount needed is about 10 - 100 mg depending on the KD.

The properties of the analyte that are helpful in experiments are the molecular mass (should be > 5 kDa for kinetic studies) and pI. The pI should be below nine; otherwise, a lot of non-specific binding is to be expected.

Interactome’s services are tailored for each project to ensure that the objectives are met or exceeded. Experienced project teams are assigned to each study focusing on progressing projects through to results in the minimum amount of time. Our clients widely regard us as professional and attentive partners who deliver quality results.

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