SPRi-Arrayer

SPRi Arrayer

Direct contact spotting

SPRi-Arrayer is an automatic, compact and portable apparatus. It prints DNA, oligonucleotides, proteins, bacterial clones and other materials with low cross contamination using Xtend metal-ceramic capillary pins. SPRi-Arrayer includes microarray design software and is integrated with microarray image processing and data analysis tools.

 

 

Benchtop SPRi-Arrayer for printing microarrays of biological samples on glass, gold surfaces, or on membrane substrates.

  • Easy to start
  • Fast and versatile
  • Prints onto SPRi-Biochip™, SPRi-Slides or any other standard slides
  • Prints up to 400 (20x20) samples on SPRi-Slides or SPRi-Biochip™
  • Spot size : from 140 to 500 µm, depending on matrix size

 

  • Print Method: Contact printing

  • Number of printing needles: 1-16 in various patterns

  • Slide capacity: 14 slides

  • SPRi-Biochip™ capacity: 8 biochips

  • SPRi-Slide capacity: 8 slides

  • Slide locks: Independent unit

  • Needle cleaning technology: Fluid stream washing, vacuum drying

Validation of the activity of G-protein-coupled receptors (GPCRs) using SPRi
Validation of the activity of G-protein-coupled receptors (GPCRs) using SPRi
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.
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.
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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