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Instruments

General purpose, high performance and ultracentrifuges that provide superior quality, reproducibility and reliable performance.

ProteomeLab XL-A/XL-I

Native-condition characterization for accurate results every time

Beckman Coulter pioneered the field of analytical ultracentrifugation and continues to design and produce powerful, reliable, and durable instrumentation to enable academic and industrial research around the world.

By measuring proteins as interacting elements, ProteomeLab XL-A and XL-I systems accelerate the development of diagnostic markers and therapeutic targets for efficient and reliable protein characterization in solution.

Each ProteomeLab system is designed to put actionable information in your hands quickly and easily.

Applications Overview

The analytical ultracentrifuge (AUC) remains the most versatile, rigorous and accurate means for determining the molecular weight and hydrodynamic/thermodynamic properties of a protein or other macromolecule. No other technique is capable of providing the same range of information with a comparable level of precision and accuracy. Learn about AUC in our Introduction to Analytical Ultracentrifugation handbook.

Described below are some fundamental applications for the analytical centrifuge for which it is either the preferred or only method of analysis. For more detail, refer to our handbook Self-Associating Systems in the Analytical Ultracentrifuge.

Sample Purity

Sedimentation analysis has a long history in examining solution heterogeneity or polydispersity. Determining average molecular weights by AUC experiments can provide sensitive and rigorous analysis to quantify minor species and allow quantitation of the size distributions in polydisperse samples.

AUC velocity experiments also allow for rapid rigorous quantitative assessment of sample heterogeneity and analysis of purity, integrity of native structure and degree of aggregation unaffected by interactions of the macromolecules with gel matrix or support.

Molecular weight determination

The analytical ultracentrifuge is unsurpassed for directly measuring molecular weights of solutes in their native state and as they exist in solution without relying on calibration or making assumptions concerning shape. The method is applicable to molecules with molecular weights ranging from several hundreds (such as sucrose) up to many millions (for virus particles and organelles).

This method is applicable to proteins, nucleic acids, carbohydrates and other substances with absorbance (or refractive index) that differs from that of the solvent. AUC experiment methods allow for a wide variety of sample sizes (15 μL-400 μL) and a wide range of concentrations can also be used to explore macromolecules in concentrated solutions (i.e., studies of very weak interactions).

Associating Systems

Sedimentation analysis is even more valuable when analyzing molecular changes in cases where molecules associate to form more complex structures.

Detecting conformation changes

Experiments in the analytical ultracentrifuge provide sedimentation and diffusion coefficients that contain information concerning the size and shape of macromolecules and the interactions between them.

Sedimentation coefficients are particularly useful for monitoring changes in conformation in proteins and nucleic acids. Bending in nucleic acids induced by protein binding may also be amenable to study. Through the combination of several different hydrodynamic or thermodynamic measurements, it is now possible to discriminate more clearly between different idealized shapes used to model the overall shape of a macromolecule in solution.

Ligand binding

Absorbance optics are particularly well suited to studies of ligand binding. Ligands and acceptors may have different intrinsic absorbance or one of the species may be labeled with a chromophore, provided the modification does not alter the binding. Analysis can be simply done with sedimentation velocity methods when the ligand and acceptor differ greatly in sedimentation coefficient such as with small molecule-protein association, DNA-protein binding or the binding of relatively large proteins to filaments such as F-actin.

Product Features

Experience better lead optimization, improved drug candidate evaluation, and enhanced method validation with the Proteome Lab Protein Characterization System

Multiple detection systems
  • Equipped with a scanning UV/Vis detection system for low-concentration work and selectivity when detecting maximum sample absorbance
  • Rayleigh Interference Optics measure the change in refractive index resulting from changes in sample concentration for improved accuracy and increased sample flexibility  
  • Both detection systems operate sequentially on the ProteomeLab XL-I to offer the broadest spectrum of data for protein characterization in solution

Easy sample prep
  • Inject 15µL-400µL sample and reference solutions into opposing positions in the cell assembly 
  • Analyze as many as 28 different sample/reference pairs in a single run, each with a unique set of solute/solvent conditions
  • Generate data for accurate analysis in as little as 3 hours

Save time with the flow-through centerpiece assembly 
  • ​Directly inject sample and reference solutions in the cell and retrieve samples for additional analysis without the need for assembly or reassembly
  • Quickly prep runs with unique dual-opening channel design providing easy access for cleaning and rinsing

ProteomeLab XL-A/XL-I Analytical Ultracentrifuge Specifications
UNSPSC 41103900 
Height 120.7 cm (47.5") 
Width 94.0 cm (37") 
Depth 67.3 cm (26.5") 
Weight 465 Kg (1025 lbs) 

Training Courses

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Register for Onsite Training (ProteomeLab XL-A/XL-I)

Videos

  • Introduction to AUC

    Click to play  

  • The History of the Analytical Ultracentrifuge

    Click to play  

  • Webinars & Symposiums

  • Advances in Sedimentation Analysis

    Borries Demeler, PhD Director, Bioinformatics Core Facility, University of Texas Health Science Center

    Click to play  

  • Aggregation Analysis and Beyond: Analytical Ultracentrifugation in the Biopharmaceutical Industry

    Alexander Bepperling, PhD Hexal AG, Sandozg, Scientist, Biophysical Characterization

    Click to play  

  • Analysis of Particle Size Distributions by Analytical Ultracentrifugation

    Helmut Cölfen, Ph.D. University of Konstanz, Physical Chemistry

    Click to play  

  • Analytical Ultracentrifugation as a Complementary Technique for Structural Analysis of Proteins and Macromolecular Complexes

    Andrew B. Herr, Ph.D. Associate Professor in the Divisions of Immunobiology and Infectious Diseases and the Center for Systems Immunology at Cincinnati Children’s Hospital Medical Center

    Click to play  

  • Analytical Ultracentrifugation in Nanoparticle Analysis

    Joshua T. Robinson, Ph.D. Senior Development Scientist Beckman Coulter Life Sciences

    Click to play  

  • Analytical Ultracentrifugation of Carbon Nanotubes

    Jeffrey Fagan, PhD National Institute of Standards and Technology Materials Science and Engineering Division Gaithersbugh, MD

    Click to play  

  • Diversity of Cancer-Derived Extracellular Vesicles

    Dolores Di Vizio, MD, PHD Associate Professor, Cedars-Sinai Medical Center and University California, Los Angeles (UCLA), Assistant Professor, Harvard Medical School

    Click to play  

  • Exploring the Stoichiometry of Macromolecular Complexes Using Multi-Signal Sedimentation Velocity Analytical Ultracentrifugation

    Chad Brautigam, PhD Associate Professor, Biophysics, Director, Macromolecular Biophysics Resource, The University of Texas Southwestern Medical Center

    Click to play  

  • Extracellular Vesicle Isolation by Flow Cytometric Sorting and Characterization by Analytical Ultra-Centrifugation and Dynamic Light Scatter

    Carley Ross, PhD Staff Development Scientist, Beckman Coulter

    Click to play  

    The extracellular vesicle (EV) research field has dramatically increased in the last five years. Using a high-speed flow cytometric sorter, EVs may be isolated at high rates such that researchers can differentially separate, isolate and...
  • Physical and Chemical Characterization of Nanoparticle Constructs Using the Analytical Ultracentrifuge

    Osman M. Bakr Division of Physical Sciences and Engineering, King Abdullah University of Science and Technology (KAUST)

    Click to play  

  • Quantitative Determination of Reaction Stoichiometry, Interaction Energies, and Solute Masses Using Analytical Ultracentrifugation

    Dr. John Burgner Adjunct Faculty Member, Biophysics department at the Virginia Commonwealth University Medical School

    Click to play  

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