MicroCal iTC200 is designed to address the needs of today’s life science researchers. The system provides results quickly and is an essential tool for any research laboratory studying biomolecular interactions. The exceptional sensitivity and data quality provide accurate results.
Direct and label-free measurement of binding affinity and thermodynamics are obtained with MicroCal iTC200. Heat released or absorbed during biochemical binding events is measured directly, giving information relative binding affinity (KD), stoichiometry (n), enthalpy (ΔH), and entropy (ΔS). This information provides valuable insights into the mechanism of binding.
A wide range of applications can be accomplished with MicroCal iTC200 including characterization of molecular interactions of small molecules, proteins, antibodies, nucleic acids, lipids and other biomolecules, enzyme kinetics, and the effects of molecular structure changes on binding mechanism.
MicroCal™ iTC200 Features:
- All binding parameters (affinity, stoichiometry, enthalpy and entropy) in a single experment
- Quick to first results with no assay develoment, no labeling, and no immobilization
- Sensitivity to investigate any biomolecular interaction using as little as 10 µg of protein
- Exceptional data quality for sub-millimolar to picomolar binding constants
- User-friendly software for fast and accurate analysis