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Biophysical Characterization Service—Analytical Ultracentrifugation (AUC)

The CD BioSciences biophysical characterisation laboratories are equipped with state-of-the-art instruments for studying proteins, nucleic acids, lipids, and complexes. Researchers can benefit from our Analytical Ultracentrifugation (AUC)-based biophysical characterisation services.

Name of the Instrument/Platform

Analytical Ultracentrifugation (AUC)

Introduction

The XL-1 is equipped with two optical detection systems. The first is capable of reading the absorbance of a sample using a dual-beam UV/VIS spectrophotometer with monochromator. The second detection system uses a laser interferometer that records the refractive index gradients. The choice of the optical detection system depends on the sensitivity needed for the experiment, the concentration range to be used, the extinction properties of the system and the buffer properties.
Two methods used for running the analytical ultracentrifuge are sedimentation velocity and sedimentation equilibrium. In sedimentation velocity, high rotor speed sediments macromolecules to the bottom of the cell. The rate of sedimentation is dependent on the size and the shape of the protein. Sedimentation velocity experiments generally run for 6 - 12 hours. Sedimentation equilibrium experiments are run at lower rotor speeds where the process of sedimentation is balanced by diffusion. When no change in the concent

Applications

1. Determine the molar mass of proteins and complexes
2. Assess the purity of a sample
3. Determine the number of species in a sample
4. Determine the stoichiometry of complexes
5. Analysis of self- and hetero-association
6. Determine binding constants (10-3– 10-8 M)
7. Characterizes synthetic polymers, biological macromolecules, viral particles, carbohydrates and nanoparticles

Summary

The Beckman ProteomeLab XL-1 measures concentration distributions of a sample in solution in a centrifugal field. The application of centrifugal force causes a redistribution of the macromolecules and the formation of a concentration boundary that moves from the meniscus to the bottom of the cell over time. A significant strength of technique is that the properties of native proteins are studied in solution -requiring no label, chemical modification or surface interaction.

In the chemistry-biology community, our service is one of the best options for teams working on biophysical characterisation. Do not hesitate to contact us if you are interested in this.

For research use only, not intended for any clinical use.
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