The identification and quantification of proteins in biological systems at a precise moment is the main focus of proteomics. HORIBA Scientific offers a wide range of label free proteomic analytic tools that allow you to examine and detect proteins from normal, disease, and drug-treated states in cells, tissue and biological fluid in real time. Moreover, we offer sophisticated tools that perform high throughput screening of proteins against a desired target and the ability to analyze a single cell using molecular fingerprinting systems.

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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
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.
Protein A280 for Protein Concentration
The new HORIBA Duetta fluorescence and absorbance spectrometer offers many unique benefits for molecular spectroscopy. It is primarily thought of as a spectrofluorometer that combines absorbance and fluorescence spectroscopy to correct the fluorescence fingerprint for concentration-related effects. Duetta can also be used as a precise absorbance spectrometer. This application note explores the use of Duetta for a common absorbance application, the Protein A280 application.
The Detection of a Low Molecular Weight Enzyme Inhibitor using the OpenPlex™ system
The use of low molecular weight molecules in the industries of drug discovery and agri-food has become increasingly important over the course of a century of drug research and science development in agriculture and in pharmaceutical field.
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).
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
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
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
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
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.
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
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.
Stopped flow time‐resolved fluorescence study of serum albumin – curcuminoid binding
Rapid mixing accessories to perform stopped flow measurements have found application in characterizing interactions and reactions occurring in solution. Reactants are expelled from syringes, mixed and injected into a flowcell.
Plasmon enhancement of protein fluorescence by silver nanostructures
The use of metal surfaces in conjunction with fluorescence molecules employing a plasmon effect, sometimes referred to as metal enhanced fluorescence, can be advantageous because of the possible enhancement of photophysical properties. For example, the emission intensity of the fluorophore, can be improved.
Dye‐protein binding monitored in a microliter volume using timeresolved fluorescence
The potential health benefits stemming from the antioxidant activity of curcumin, commonly found in turmeric (Curcuma longa L), has attracted the interest of several research groups.
Selective excitation of tryptophan fluorescence decay in proteins using a subnanosecond 295 nm light-emitting diode and time-correlated single-photon counting
We demonstrate an AlGaN light-emitting diode (LED) giving pulses of ~600 ps full width half maximum, 0.35 µW average power, 0.6 mW peak power, and ~12 nm bandwidth at 295 nm. This source is ideal for protein intrinsic tryptophan fluorescence decay research without the unwanted excitation of tyrosine and paves the way to lab-on-a-chip protein assays using fluorescence decay times. Fluorescence decay and anisotropy decay measurements of human serum albumin are reported and the usefulness of the 295 nm LED demonstrated in comparisons with a nanosecond flashlamp and LEDs with nominal wavelength emission of 280 nm.
Fluorescence Anisotropy Studies
Polarized light striking a fluorescent molecule results in polarized fluorescence. This polarized emission gradually returns to unpolarized fluorescence depending on rotational diffusion and other factors. Anisotropy is directly related to the polarization, and is the ratio of the polarized light component to the total light intensity.


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