Aptamer Validation
At NeoVentures Biotechnology Inc., we combine deep expertise in aptamer science with advanced biophysical instrumentation to provide precise, quantitative validation of aptamer–target interactions.
Using Isothermal Titration Calorimetry (ITC) and Surface Plasmon Resonance Imaging (SPRi), we measure affinity, kinetics, and thermodynamics, giving you a complete picture of how your aptamer performs under real-world conditions.
Our comprehensive approach ensures that your aptamer validation is scientifically rigorous, reproducible, and ready for both research and commercial applications.
Why Choose NeoVentures Biotechnology?
Proven expertise in aptamer biophysics and assay development.
State-of-the-art instrumentation and proprietary analysis tools.
Customizable validation packages for all project sizes.
Fast turnaround and responsive collaborator.
Our Validation Workflow
1. Consultation
2. Sample Preparation
3. Aptamer Validation
4. Data Analysis
5. Support
Isothermal Titration Calorimetry (ITC)
Label-free, solution-based thermodynamic profiling
ITC directly measures the heat released or absorbed during aptamer–target binding, providing a full thermodynamic signature of the interaction. This technique delivers unmatched accuracy without the need for labeling or immobilization.
Key Advantages:
- Quantitative determination of binding constants (Kd)
- Full thermodynamic characterization (ΔH, ΔS, n)
- No labeling or immobilization required
- Suitable for proteins, peptides, and small molecules
Surface Plasmon Resonance Imaging (SPRi)
Real-time kinetic and affinity analysis
SPRi enables label-free, real-time monitoring of aptamer–target interactions on a sensor surface. It provides detailed kinetic data, association (kon) and dissociation (koff) rates, as well as equilibrium affinity values.
Key Advantages:
- Real-time monitoring of binding events
- Determination of kinetic parameters (kon, koff)
- Multiplexed analysis for high-throughput screening
- Minimal sample consumption
Aptamer Validation Options
Inclut :
- – Real-time monitoring of association and dissociation events
- – Determination of kinetic rate constants (kon, koff) and equilibrium affinity (Kd)
- – Comparative binding analysis for multiple aptamer sequences (multiplexed format)
- – Sensorgram plots and detailed data report
- – Interpretation and summary of results, including recommendations for next steps
Best for: Screening aptamer candidates, comparing affinities, or optimizing sequence performance.
Inclut :
- – Quantitative determination of binding affinity (Kd)
- – Full thermodynamic characterization (ΔH, ΔS, and stoichiometry)
- – Assessment of binding mechanism and molecular interaction strength
- – Graphical output and data report
- – Expert interpretation of the thermodynamic profile
Best for: Confirming binding in solution, characterizing binding mechanisms, or validating aptamer performance under native conditions.
Comprehensive Kinetic and Thermodynamic Validation
For the most complete understanding of your aptamer-target interaction, a combination of SPRi and ITC provides both kinetic and thermodynamic data, enabling robust validation across multiple parameters.
You will receive:
- – Full kinetic and thermodynamic characterization (kon, koff, Kd, ΔH, ΔS, n)
- – Cross-validation of affinity measurements between methods
- – Comparative insights into binding behavior in both immobilized and solution-based systems
- – High-confidence confirmation of aptamer functionality and performance
- – Detailed technical report with data interpretation and recommendations
Best for: Final validation of aptamers intended for diagnostic, therapeutic, or biosensor applications where performance confidence is essential.
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