Proteomics

Proteomics

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.

Browse Application

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.
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
SPRi Imaging of oligosaccharides proteins 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
Label-free Ligand Fishing in Human Plasma
Interaction between immobilized peptides and protein from sera on Cystamine / Glutaraldehyde functionalized biochip
Detection of birch pollen allergen in the air
Antibody-Antigen Specific interaction
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
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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