Close

Search

Search Menu
Photonics Media Photonics Buyers' Guide Photonics EDU Photonics Spectra BioPhotonics EuroPhotonics Industrial Photonics Photonics Showcase Photonics ProdSpec Photonics Handbook
More News
share
Email Facebook Twitter Google+ LinkedIn

Calypso CG-MALS System

Photonics.com
Sep 2011
Wyatt Technology Corp.Request Info
 
SANTA BARBARA, Calif., Sept. 8, 2011 — Wyatt Technology Corp. has released the Calypso, a composition-gradient multiangle light-scattering (CG-MALS) system that achieves accurate measurements of biomolecular interactions.

It can determine both the affinity and binding stoichiometry for macromolecules in solution, with no need for sample tagging or immobilization that could influence the interaction. 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 and field flow fractionation MALS, have been used to study interactions, but they have limitations. As the molecules become separated in the course of dilution and fractionation, they no longer interact. And, upon reaching the detectors, the molecules often are not in equilibrium, nor in a well-defined kinetic state.

Calypso complements traditional MALS separation techniques, keeping the molecules in proximity to probe their interactions. The analyzer was used in conjunction with an online ultraviolet/visible concentration detector and the proprietary Dawn Heleos MALS instrument to provide rapid and precise measurements of the interaction between an antithrombin antibody and human thrombin α. The equilibrium dissociation constant determined by the system agreed well with the manufacturer’s data as measured by ELISA.

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 various composition or concentration to characterize macromolecular interactions, including reversible self- and heteroassociation of proteins, reaction rates and affinities of irreversible aggregation, and virial coefficients. No special modifications are required. Instead, samples are unlabeled and entirely in solution. Calypso’s automation capabilities enhance productivity by improving repeatability and reliability, while minimizing time and effort.


REQUEST INFO ABOUT THIS PRODUCT

* Message:
(requirements, questions for supplier)
Your contact information
* First Name:
* Last Name:
* Email Address:
* Company:
Address:
Address 2:
City:
State/Province:
Postal Code:
* Country:
Phone #:
Fax #:

Register or login to auto-populate this form:
Login Register
* Required

When you click "Send Request", we will record and send your personal contact information to Wyatt Technology Corp. by email so they may respond directly. You also agree that Photonics Media may contact you with information related to this inquiry, and that you have read and accept our Privacy Policy and Terms and Conditions of Use.
MORE FROM PHOTONICS MEDIA
Test & Measurement
AmericasBiophotonicsCaliforniaCalypso GC-MALS systemcomposition-gradient multiangle light-scattering systemdetermine affinity and binding stoichiometryinteraction antithrombin antibody and human thrombin ameasure biomolecular interactionsProductsreversible heteroassociationreversible self-associationSensors & DetectorsTest & Measurementunfractionated samples characterize macromolecular interactionsvirial coefficientsWyatt Technology

Terms & Conditions Privacy Policy About Us Contact Us
back to top
Facebook Twitter Instagram LinkedIn YouTube RSS
©2018 Photonics Media, 100 West St., Pittsfield, MA, 01201 USA, info@photonics.com

Photonics Media, Laurin Publishing
x We deliver – right to your inbox. Subscribe FREE to our newsletters.
X
Are you interested in this product?
When you click "Send Request", we will send the contact details you supply to Wyatt Technology Corp. so they may respond to your inquiry directly.

Email Address:
Name:
Company:
Stop showing me this for the remainder of my visit
We use cookies to improve user experience and analyze our website traffic as stated in our Privacy Policy. By using this website, you agree to the use of cookies unless you have disabled them.