We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience. You can read our Cookie Policy here.

Advertisement
Wyatt Technology’s Calypso GC-MALS System Provides Fast and Accurate Measurements of Biomolecular Interactions
Product News

Wyatt Technology’s Calypso GC-MALS System Provides Fast and Accurate Measurements of Biomolecular Interactions

Wyatt Technology’s Calypso GC-MALS System Provides Fast and Accurate Measurements of Biomolecular Interactions
Product News

Wyatt Technology’s Calypso GC-MALS System Provides Fast and Accurate Measurements of Biomolecular Interactions


Want a FREE PDF version of This Product News?

Complete the form below and we will email you a PDF version of "Wyatt Technology’s Calypso GC-MALS System Provides Fast and Accurate Measurements of Biomolecular Interactions"

First Name*
Last Name*
Email Address*
Country*
Company Type*
Job Function*
Would you like to receive further email communication from Technology Networks?

Technology Networks Ltd. needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy

Wyatt Technology Corporation, has announced that its Calypso Composition-Gradient Multi-Angle Light Scattering (CG-MALS) system achieves accurate measurements of biomolecular interactions.

The Calypso offers the unique capability of determining both the affinity and binding stoichiometry for macromolecules in solution with no need for immobilization or tagging, which may influence the interaction.

This is demonstrated in a new application note, titled “Measuring Antibody-Antigen Interactions with the Calypso”, which is available to download free-of-charge via http://www.wyatt.com/files/literature/Calypso-Measuring_Antibody-Antigen_Interactions.pdf.

Antibody-antigen binding, hormone-receptor interactions and many other common biomolecular interactions occur at stoichiometries other than 1:1.

Conventional separation techniques, such as size exclusion chromatography MALS (SEC MALS) and field flow fractionation MALS (FFF MALS) have been extensively used to study interactions, however they are associated with certain important limitations.

As the molecules become separated in the course of dilution and fractionation, they no longer interact. Additionally, upon reaching the detectors, the molecules are often not in equilibrium, neither are they in a well defined kinetic state.

The new application note illustrates how Calypso complements traditional MALS separation techniques, keeping the molecules in close proximity to probe their interactions.

The analyzer was used in conjunction with an online UV/Vis concentration detector and Wyatt’s DAWN HELEOS MALS instrument to provide rapid and precise measurements of the interaction between an anti-thrombin antibody (Ab) and human thrombin α (Thr).

The equilibrium dissociation constant determined by the system agreed well with the manufacturer’s data as measured by ELISA.

In addition, both thrombin and the antibody exhibited no propensity for self-association, a finding that could not be evaluated by conventional ELISA.

Calypso employs a series of unfractionated samples of different composition or concentration in order to characterize macromolecular interactions, including reversible self- and hetero-association of proteins, reaction rates and affinities of irreversible aggregation, and virial coefficients.

No special modifications, such as sample tagging or immobilization procedures, are required. Instead, samples are unlabeled and entirely in solution.

Furthermore, Calypso’s automation capabilities enhance productivity by improving repeatability and reliability, while minimizing time and effort.

Advertisement