XelPleX

XelPlex

Fully automated label-free molecular interaction analysis machine One System for Molecule Screening & Crude Sample Analysis

 

XelPleX is a high-performance and fully automated instrument for the analysis of label-free biomolecular interactions in a multiplex format.

The array-based format of the sensor chips allows you to monitor up to several hundreds interactions simultaneously and to accelerate your research.

The optimized fluidic system is designed to give you full kinetic profiles within minutes and help you make the right decisions quickly and with confidence.

XelPleX is powered with EzSuite, our new software suite for simple use and advanced data analysis.

Segment: Scientific
Manufacturing Company: HORIBA France SAS

Automated SPR imaging system for label-free assays:

  • Multiplex Detection of several hundred interactions
  • Label-Free protein, peptide, DNA samples
  • Real-Time monitoring of kinetic curves
  • Difference Image Display giving you a direct view of reactions as the experiment unfolds
  • Fast Total Assay Time - typical assays in less than 10 minutes
  • Temperature control
  • Sample recycling for maximum binding
  • Sample recovery function
  • Direct subtraction of the negative control

 

 

 

  • Sample volume: typically 200 μL
  • Sample concentration: 150 ng/mL (100-1000 kDa) to 5 μg/mL (4-20 kDa)
  • Sample molecular weight: ≈150 Da
  • Limit of detection: 5 pg/mm2
Production of a single domain antibody Q17c directed against recombinant HER2 protein and its binding study by Surface Plasmon Resonance imaging technology
Production of a single domain antibody Q17c directed against recombinant HER2 protein and its binding study by Surface Plasmon Resonance imaging technology
This application note shows how binding kinetics of single-domain antibodies can be studied with SPRi technology. QVQ produces single-domain antibodies from camelids (sdAbs or VHH). Like conventional Abs, sdAbs are able to bind specific epitopes with high binding affinity. The small size of sdAbs allows for enhanced tumor penetration and fast blood clearance, features that are favorable for in vivo imaging applications. Here, the binding of the anti-HER2 sdAb Q17c to recombinant HER2 protein was assessed using Surface Plasmon Resonance imaging (SPRi). An optimization of immobilization conditions was performed for Q17c and its specific antigen HER2 using a single SPRi-Biochip.
Production of a rescued recombinant monoclonal antibody directed against a steroid hormone and its binding study thanks to Surface Plasmon Resonance imaging technology
Production of a rescued recombinant monoclonal antibody directed against a steroid hormone and its binding study thanks to Surface Plasmon Resonance imaging technology
A monoclonal antibody (mAb) highly specific to a steroid hormone (undisclosed) of 290 Daltons was analyzed thanks to SPRi technology. This application note highlights the sensitivity of the XelPleXTM system for the detection of small molecules.
Streamlined SPRi-MS coupling to detect and identify a kinase in Cell lysate using the DARPins as binders
Streamlined SPRi-MS coupling to detect and identify a kinase in Cell lysate using the DARPins as binders
DARPins (Designed Ankyrin Repeat Proteins) are a class of non-immunoglobulin binders. Thanks to their specificity and robustness, they allow a multitude of novel, so far unfeasible applications. Surface Plasmon Resonance imaging (SPRi) is a powerful label-free technique that enables real-time target detection. Combining SPRi to massspectrometry (MS) allows biomolecules identification using their unique peptide mass fingerprint. In the past this combination was cumbersome and time-consuming. This application note shows how a protein kinase (RPS6KA2), a potential drug target is detected and identified using a hyphenated On-Chip SPR-MS coupling protocol, leading to saving time and money.
Validation of the activity of G-protein-coupled receptors (GPCRs) using SPRi
Validation of the activity of G-protein-coupled receptors (GPCRs) using SPRi
The Detection of an Ultralow Molecular Weight Enzyme Inhibitor using the XelPleX system
The Detection of an Ultralow Molecular Weight Enzyme Inhibitor using the XelPleX system
Detection of low molecular weight molecules can be useful especially for pharmaceutical and agri-food applications. This application note is focused on the detection of a 157 Dalton molecule, the benzenesulfonamide, using the XelPleX system. The benzenesulfonamide is an inhibitor of the human carbonic anhydrase enzyme type II (CAII).
Rapid couplig of SPRi and proteinchip
Rapid couplig of SPRi and proteinchip
Real time detection of lymphocytes with SPRi
Real time detection of lymphocytes with SPRi
SPRi Imaging of oligosaccharides proteins interactions
SPRi Imaging of oligosaccharides proteins interactions
The majority of proteins are glycosylated: they possess oligosaccharide chains and are hence termed glycoproteins. Oligosaccharides, also called carbohydrate or sugar, are often quite large (as large as some protein domains for example) and they have many functions in molecular interactions.
Protein-Peptide interactions studies with SPRi
Protein-Peptide interactions studies with SPRi
Description of the advantages of combining the use of peptide chips with direct label-free detection as achieved by SPR imaging (SPRi).
Monitoring of interactions between aptamers and human IgE by SPRi
Monitoring of interactions between aptamers and human IgE by SPRi
This application note shows that the HORIBA Scientific SPRi platform is suitable for the analysis of aptamer-based molecular interactions. For this purpose, the interaction between human IgE protein, an antibody involved in allergic reactions, and a human IgE specific aptamer4 is presented as proof-of-concept.
Label-free Ligand Fishing in Human Plasma
Label-free Ligand Fishing in Human Plasma
Surface Plasmon Resonance (SPR) is an optical technique that offers label-free biomolecular analyses, providing information on kinetic processes (association and dissociation), binding affinity, analyte concentration and real time molecule detection. It has become a powerful tool for the analysis of biomolecular events involved in drug development, cancer research, and antibody screening, ...
Interaction between immobilized peptides and protein from sera on Cystamine / Glutaraldehyde functionalized biochip
Interaction between immobilized peptides and protein from sera on Cystamine / Glutaraldehyde functionalized biochip
Our SPRi technology (Surface Plasmon Resonance imaging), is able to measure multiplexed label-free biolo-gical interactions in a complex media such as serum.We will demonstrate the ability to monitor specific interactions between immobilized peptides and proteins issued from non purified immune sera, using a cystamine/glutaraldehyde SAM surface chemistry on the bio-chip surface. We chose to illustrate this ability by monitoring the interaction between an ovalbumin peptide fragment and an ovalbumin immunized serum.
How to quantify a protein in different crude samples in one run, using the XelPleX
How to quantify a protein in different crude samples in one run, using the XelPleX
Detection of birch pollen allergen in the air
Detection of birch pollen allergen in the air
The purpose of this proof of concept is to show that Surface Plasmon Resonance imaging (SPRi) is a suitable technique to detect allergens. Compared with other techniques, such as ELISA or Luminex, which are based on colorimetric or fluorescence detection, this technology does not require the labeling of antibodies.
Antibody-Antigen Specific interaction
Antibody-Antigen Specific interaction
HORIBA provides the pharmaceutical industry, biotech companies and academic research laboratories with high performance instrumentation based on SPRi technology (Surface Plasmon Resonance imaging). To demonstrate the power of this technology, we carried out an experiment based on an antibody-antigen interaction. Original surface chemistry combined with an electrochemical process allows the rapid coupling of biomolecules to the gold layer (polypyrrole co-polymerisation) on the top of a glass prism.

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