Related Experiment Video
Updated: Sep 17, 2025
10:49
Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
Published on: September 20, 2016
12.8K
SNAP-tag2 for faster and brighter protein labeling
Stefanie Kühn1, Veselin Nasufovic1, Jonas Wilhelm1
1Department of Chemical Biology, Max Planck Institute for Medical Research, Heidelberg, Germany.
Nature Chemical Biology
|July 3, 2025
Summary
Researchers developed SNAP-tag2, an improved protein labeling system. It offers faster labeling and brighter fluorescence for enhanced bioimaging in live cells and super-resolution microscopy.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioimaging
Background:
- SNAP-tag is a widely used protein labeling tool in bioimaging.
- Limitations include slow labeling kinetics and poor substrate cell permeability for live-cell applications.
Purpose of the Study:
- To engineer an improved SNAP-tag system for faster and brighter protein labeling.
- To enhance live-cell and super-resolution imaging capabilities.
Main Methods:
- Development of an engineered SNAP-tag variant (SNAP-tag2).
- Design of novel labeling substrates.
- Kinetic analysis of labeling reactions.
- Assessment of fluorescence brightness and live-cell imaging performance.
Main Results:
- SNAP-tag2 achieved a 100-fold increase in labeling rate constants with rhodamine substrates compared to SNAP-tag.
- SNAP-tag2 demonstrated a fivefold increase in fluorescence brightness with fluorogenic dyes.
- Improved performance in live-cell and super-resolution imaging applications.
Conclusions:
- SNAP-tag2 significantly enhances protein labeling efficiency and brightness.
- This advancement expands the utility of SNAP-tag technology for demanding live-cell imaging studies.
Related Concept Videos
01:19Protein Dynamics in Living Cells
2.3K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.3K
03:31Labeling DNA Probes
8.4K
DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
8.4K
01:24Tagging and Fusion Proteins
6.9K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
6.9K