ZEISS Spectral RICS​
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ZEISS Spectral RICS​

Mapping Molecular Interactions in the Cellular Environment ​

ZEISS Spectral RICS combines LSM imaging with information about the behavior of proteins in their cellular environment. This integrated approach facilitates the identification of regions exhibiting diverse molecular characteristics. Uniquely, through spectral unmixing, Spectral RICS provides an optimal foundation for investigating protein-protein binding behavior.

  • Obtain unbiased information of protein interaction
  • Explore their mobility within the cellular context
  • Integrate confocal imaging with molecular characteristics
Raw time series (left) and grid heatmap (right). The RICS analysis reveals that EGFP diffusion is slower inside the nucleoli compared to the nucleoplasm. Sample kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany.
Raw time series (left) and grid heatmap (right). The RICS analysis reveals that EGFP diffusion is slower inside the nucleoli compared to the nucleoplasm. Sample kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany.

Raw time series (left) and grid heatmap (right). The RICS analysis reveals that EGFP diffusion is slower inside the nucleoli compared to the nucleoplasm. Sample kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany.

Raw time series (left) and grid heatmap (right). The RICS analysis reveals that EGFP diffusion is slower inside the nucleoli compared to the nucleoplasm. Sample kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany.

Raster Imaging Correlation Spectroscopy

Study the Dynamics of Molecules at the Cellular Level​

Raster Imaging Correlation Spectroscopy (RICS) is an advanced technique used in biological imaging to study the dynamics of molecules and particles at the cellular level. It involves analyzing the movement of fluorescently labeled particles across a raster-scanned image of a sample. By correlating the intensity fluctuations between different pixels in the image, RICS can provide information about the diffusion rates, concentration, and interactions of these particles.

An assumed interaction between two proteins could be proven to be non-existent with RICS analysis after spectral unmixing.
An assumed interaction between two proteins could be proven to be non-existent with RICS analysis after spectral unmixing.

An assumed interaction between two proteins could be proven to be non-existent with RICS analysis after spectral unmixing. Sample kindly provided by Prof. Jelle Hendrix, Dynamic Bioimaging Lab, Advanced Optical Microscopy Centre, Biomedical Research Institute, Hasselt University.

An assumed interaction between two proteins could be proven to be non-existent with RICS analysis after spectral unmixing. Sample kindly provided by Prof. Jelle Hendrix, Dynamic Bioimaging Lab, Advanced Optical Microscopy Centre, Biomedical Research Institute, Hasselt University.

The Advantage of Spectral RICS

Uncover the True Behavior of Proteins in Living Cells

ZEISS Spectral RICS has been developed in collaboration with Prof. Jelle Hendrix, Hasselt University, Belgium. It adds spectral unmixing to the RICS method, helping you to avoid the misinterpretation of overlapping spectra as protein interactions. With unmixed spectra, you can be sure to obtain unbiased information and reveal the true behavior of proteins in living cells.​

ZEISS Spectral RICS comes as a workflow-based ZEN extension, guiding you from experiment setup to data analysis. It includes spectral unmixing, auto and cross correlation analysis, intensity and grid heatmaps, and time-depended analysis, combined with tools such as ROI selection and intensity thresholding.

ZEISS Spectral RICS Application Examples​

Effects of SUMOylation in protein diffusion
Effects of SUMOylation in protein diffusion

Samples kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany

Samples kindly provided by P. Hemmerich and T. Ulbricht, Core Facility Imaging, Leibniz Institute on Aging, Jena, Germany

Effects of SUMOylation in protein diffusion

RICS can be used to measure changes in diffusion resulting from protein interaction. With standard auto-correlation RICS analysis, we can see that the diffusion coefficient drops in correspondence with the size of SUMO chain. This type of studies can also measure the changes in diffusion of tagged proteins of interest in the presence of drug treatments, mutations, or other influences.

Interaction of LEDGF with histones
Interaction of LEDGF with histones

Sample kindly provided by Prof. Jelle Hendrix, Dynamic Bioimaging Lab, Advanced Optical Microscopy Centre, Biomedical Research Institute, Hasselt University, Belgium

Sample kindly provided by Prof. Jelle Hendrix, Dynamic Bioimaging Lab, Advanced Optical Microscopy Centre, Biomedical Research Institute, Hasselt University, Belgium

Interaction of LEDGF with histones

LEDGF is a chromatin binding transcription factor, and H2B is a histone that helps organize eukaryotic DNA. Before spectral unmixing, RICS cross-correlation analysis of the 2 proteins shows strong interaction. However, spectral unmixing reveals that in most of the nucleus the interaction of the two proteins in very small.

Exploring the behavior of EGFR at reoviral docking sites
Exploring the behavior of EGFR at reoviral docking sites

Sample kindly provided by J.D. Simpson & D. Alsteens, NanoBiophysics lab, UC Louvain, Belgium​

Sample kindly provided by J.D. Simpson & D. Alsteens, NanoBiophysics lab, UC Louvain, Belgium​

Exploring the behavior of EGFR at reoviral docking sites​

Epidermal Growth Factor Receptor (EGFR) is expressed on the membrane of cells and is one of the entry receptors for reoviruses. The reoviral landing and docking sites are visualized in magenta. RICS analysis depicted as a grid-based heatmap reveals that the diffusion of EGFR is faster adjacent to the viral docking sites, compared to other membrane locations.

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      Your Solution for Mapping Molecular Interactions in the Cellular Environment

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