In-gel Fluorescence
In-gel Fluorescence - Related Videos
05:03
Fluorescent Silver Staining: A Technique to Visualize Total Protein in Polyacrylamide Gels
0 Views •
2025
In this video, we demonstrate a silver staining method of polyacrylamide gels for the visualization of total protein by using fluorogenic probes.
06:24
Fluorescent Silver Staining of Proteins in Polyacrylamide Gels
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Cited by 7 •
2019
Here, we describe a detailed protocol outlining a new fluorescent staining technique for total protein detection in polyacrylamide gels. The protocol utilizes a silver ion-specific fluorescence turn-on probe, which detects Ag+-protein complexes, and eliminates certain limitations of traditional chromogenic silver stains.
06:41
Light Sheet Fluorescence Microscopy of Plant Roots Growing on the Surface of a Gel
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Cited by 24 •
2017
This protocol shows a plant sample preparation method for light-sheet microscopy. The setup is characterized by mounting the plant vertically on the surface of a gel and letting it grow in controlled bright conditions. This allows long-term observation of plant organ development in standardized conditions.
10:55
Staining Proteins in Gels
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Cited by 7 •
2008
Following separation by electrophoretic methods, proteins in a gel can be detected by several staining methods. Staining of proteins with Coomassie Blue, Silver Staining, SYPRO Orange, SYPRO Ruby are demonstrated in this video.
03:05
Fluorescent Peptide Zymography: A Modified Technique to Detect Protease Activity Using Fluorogenic Substrates in Zymogram Gels
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2025
In this video, we perform zymography, an electrophoretic technique, to analyze the proteolytic activity within biological samples.
FAQs
Fluorescent molecules are detected through the relationship between excitation and emission. Illumination at an appropriate excitation wavelength causes the labeled molecule or reporter to produce emitted light. That light identifies where the material is located in the gel, so the resulting pattern can be examined for the positions of separated biological components and their relative signal levels.
Preserving the sample’s location in the gel links the fluorescent signal to electrophoretic migration. Researchers can therefore relate a visible signal to the position reached by a protein, nucleic acid, or reporter during separation, rather than first moving the material to another surface. This spatial continuity helps maintain information about how the separated components are distributed.
In-gel fluorescence can support analysis of fluorescently labeled proteins, nucleic acids, and fluorescent reporter molecules. It is also relevant when studying fluorescent fusion proteins, where a fluorescent component is associated with a protein of interest. Selecting among these sample types allows the same imaging principle to serve protein analysis, nucleic acid separation, or reporter-based biological investigations.
A basic workflow begins by running the labeled biological sample through electrophoresis so its components migrate through the gel. The gel is then illuminated at an excitation wavelength, and the emitted light is used to visualize the separated signals. Researchers can analyze those locations directly, avoiding the need to transfer the sample to another surface before imaging.
It is useful when researchers need to examine separated proteins or nucleic acids while retaining their positions in the gel. The technique can fit workflows that also assess fluorescent reporter molecules or fusion proteins. Because it can reduce additional staining or processing steps, it offers an efficient option for visualizing labeled material after electrophoretic separation.
Signal position indicates where a fluorescent component migrated, while the amount of emitted light can support comparison of relative abundance. These measurements preserve both separation and signal information in the gel. The approach is therefore useful for visualizing distributions and comparing labeled biological material, with sensitivity and efficiency serving as practical benefits.