Protein Characterization Systems / Protein Analysis Systems

The ProteomeLab™ XL-A provides thermodynamic and hydrodynamic information about macromolecules in solution. The computer-controlled system collects absorbance data from sedimentation equilibrium and sedimentation velocity experiments. The XL-A Windows User Interface and Data Analysis Software, included with each ProteomeLab™ XL-I and XL-A, interprets the data to provide information about association states of interacting molecules, association constants, weight average molecular weight, sedimentation and diffusion coefficients and conformation changes. These systems are capable of running up to 21 samples using the appropriate cell assemblies and rotor. Basic hands-on instrument and software training is provided with the purchase of an ProteomeLab™ XL-A or XL-I.

Includes:

• An-60 Ti 4-hole rotor
• 1 assembled cell (flow through centerpiece, quartz windows)
• Counterbalance set
• Torque stand
• Accessory kit (includes start-up kit)

The ProteomeLab™ XL-I features dual integrated optical systems that include Rayleigh Interference optics and scanning UV/Visible optics. The Rayleigh Interference system extends the working concentration range of the analytical ultracentrifuge, and is ideal for samples that do not absorb in the UV/Visible range such as polysaccharides, carbohydrates, and polymers. The XL-A Windows User Interface and Data Analysis Software, included with each ProteomeLab™ XL-I and XL-A, interprets the data to provide information about association states of interacting molecules, association constants, weight average molecular weight, sedimentation and diffusion coefficients and conformation changes.These systems are capable of running up to 21 samples using the appropriate cell assemblies and rotor. Basic hands-on instrument and software training is provided with the purchase of an ProteomeLab™ XL-A or XL-I.

Includes:

• An-50 Ti 8-hole rotor
• 3 assembled cell (flow through centerpiece, quartz windows)
• Counterbalance set
• Torque stand
• Accessory kit (includes start-up kit)

The iCE280 performs free solution IEF in a capillary column (cIEF) and detects focused protein zones using a whole column UV absorption detector that avoids disturbing the focused zones. Focusing begins when voltage is applied to a 50-mm transparent capillary loaded with sample and ampholytes. A CCD camera takes a UV light absorption image of the whole capillary column every 30 seconds. The resulting separation pattern is then analyzed. Whole column imaged detection eliminates the need for a mobilization step which is required in traditional capillary isoelectric focusing. The mobilization step contributes both time and complexity to method development.

The elimination of this step provides:
* Rapid sample analysis 3 to 10 times faster than traditional cIEF and ion exchange chromatography.
* Method development reduced from months to hours —glycosylated protein separations can be developed in as little as 4 hours, monoclonal antibody methods in as little as 1 hour.
* Excellent resolution and reproducibility to facilitate stability studies and product identification assays

• Profile and compare hundreds of interactions in parallel and in real timewithout labeling
• Select interactions of interest for downstream characterization
• Map biomolecular interaction networks and understand their functions
• Define epitopes and discover new biomarkers
• Get more and new information in less time compared to classical assay formats
• Versatile instrument with straightforward assay set up
• Immobilise material such as proteins, peptides, nucleic acids, and carbohydrates,and see the interactions with agents such as proteins, viruses, bacteria and mammalian cells.
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• one platform for highest quality comprehensive characterization - kinetics,affinity, specificity, concentration and thermodynamics
• Confident selection and characterization of therapeutic candidates
• Define potential drug targets and diagnostic markers
• Optimize safety and efficacy – detect and characterize immune response in immunogenicity studies and immunotherapeutic development
• Increase understanding of molecular mechanism, structure-functionrelationships and interaction profiles