ProteomeLab™ XL-A/XL-I

ProteomeLab™ XL-A/XL-I

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BECKMAN COULTER. Native-condition characterization for better lead optimization, better drug candidate evaluation, better method validation....better science.

Consulte
The ProteomeLab XL-A/XL-I in-solution characterization of proteins, oligomers, aggregates, particles, colloids, and small structures delivers accurate results you can rely on time and again. In-solution characterization allows for testing in native conditions, meaning you determine the sample testing environment that best suits your needs. The unique column-free separating technique of the ProteomeLab XL-A/XL-I measures the relative change in the distribution of molecular weights, providing an efficient way to measure heterogeneity, stoichiometry and self-associating systems. And, because the measurements are based on the first principles of thermodynamics and hydrodynamics, no standards or calibrations are required. As a result, you spend less time on setup and more time on discovery.

Our analytical ultracentrifuge platform offers a variety of customizable options, to meet your needs.  Sensitive absorbance optics enable analysis of most samples, and interference optics can be used for low concentrations.  Both systems can be implemented simultaneously, to maximize data acquisition in a single run.  Additionally, we offer two different rotor configurations, and a variety of cell types, to enable multiple experimental designs.  The wide range of rotational velocities also allow investigators to probe protein size, dimerization, and binding constants.
As mentioned, the analytical ultracentrifuge can be used for several types of experiments, but the two most widely used are sedimentation velocity and sedimentation equilibrium.  Sedimentation velocity experiments are utilized to determine protein molecular weight and identify degree of dimerization.  In a sedimentation velocity experiment, high rotor speeds are used to completely sediment all particles in solution.  Protein dimers sediment at a different rate than single protein molecules owing to their higher weight, and since the analytical ultracentrifuge measures protein formulations in their native state, the degree of dimerization can be assessed to highly accurate levels. 

Sedimentation equilibrium experiments use lower velocity, and assess the concentration distribution as a function of g-force applied.  By measuring the concentration curve at several different g-forces, equilibrium binding constants can be measured.  This approach provides several advantages to alternative technologies, which often require immobilization of one binding partner, and thus, can impact equilibrium binding by modify the conformation of the immobilized protein.

The analytical ultracentrifuge can also be used for high resolution size analysis of particles, and has been applied to samples as diverse as quantum dots, polymer nanoparticles, and carbon nanotubes.  Since the instrument performs both separation and detection in a single experiment, it provides many advantages over ensemble techniques such as light scattering.  Mass proportional size distributions can be obtained, which cannot be measured with ensemble approaches.

Beckman Coulter pioneered the field of analytical ultracentrifugation, with the first commercial model, and has continued to supply the field with high quality, powerful, and reliable instrumentation for several decades.  Our current instruments continue this history of innovation, and are relied upon by academic and industrial customers throughout the world.

FEATURES:

Multiple Detection Systems

The ProteomeLab XL-A is configured with a scanning UV/Vis detection system that provides sensitivity for low-concentration work and selectivity for optimizing detection based on the sample's maximum absorbance. The addition of Rayleigh Interference Optics provides the capability to measure the change in refractive index resulting from changes in sample concentration. This delivers increased accuracy and the ability to examine a greater concentration range with a wider selection of samples. The XL-I can collect data from both detection systems sequentially, to provide the broadest spectrum of data for protein characterization in solution.

Easy Sample Preparation

For easy sample preparation, inject as little as 15µL to 120µL of sample and reference solutions into opposing positions in the cell assembly, and place the assembly into the system. Up to 28 different sample/reference pairs can be studied in a single run, with each having a different set of solute/solvent conditions (pH, ionic strength, concentration). This provides data for accurate analysis in as little as three hours. Your sample can be retrieved for additional analysis.

Flow-Through Centerpiece Assembly

A pre-assembled cell features a flow-through centerpiece that saves you time. Sample and reference solutions can be directly injected in the cell and retrieved for additional analysis without assembling or disassembling the cell. A second hole above each channel allows the cell to be cleaned and rinsed (with tubing and syringe) and ready for the next run.

SPECIFICATIONS:

UNSPSC: 41103900
Height: 120.7 cm (47.5 in.)
Width: 94.0 cm (37 in.)
Depth: 67.3 cm (26.5 in)
Weight: 465 Kg (1025 lb)

Availability of rotors, parts and accessories.