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Labeling DNA Probes

Labeling DNA Probes

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...

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Updated: Sep 16, 2025

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

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Published on: August 4, 2021

On-Demand Proximity Labeling Using Light-Activated BioID.

Carolyn Marie Orduno Davis¹, Sanjeevi Sivasankar²

¹Department of Biomedical Engineering, University of California, Davis, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)

|July 10, 2025

Summary

This summary is machine-generated.

We developed Light-Activated BioID (LAB), a novel tool for mapping membrane protein interactions. LAB uses light to control proximity biotinylation, overcoming limitations of existing methods for precise protein interaction studies.

Keywords:

BioID Light activation Membrane proteins Optogenetics Proteomics Proximity biotinylation Proximity labeling TurboID

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Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

Area of Science:

Proteomics
Molecular Biology
Biochemistry

Background:

Membrane proteins are crucial for tissue structure and function.
Traditional proteomic methods struggle to map membrane protein interactomes.
Existing proximity labeling tools like TurboID lack on-demand control, leading to background noise.

Purpose of the Study:

To develop a light-activated proximity labeling technology for precise mapping of membrane protein interactions.
To overcome the limitations of continuous labeling methods.
To enable spatial and temporal control over biotinylation for interactome mapping.

Main Methods:

Developed Light-Activated BioID (LAB) by combining split-TurboID enzyme with photodimeric CRY2 and CIB1 proteins.
Engineered a light-controlled proximity biotinylation system.
Tested and utilized LAB for mapping membrane protein-protein interactions (PPIs).

Main Results:

LAB provides user-controlled, light-activated proximity biotinylation.
Achieved high spatial and temporal resolution in mapping membrane PPIs.
Demonstrated the utility of LAB for studying membrane-bound protein interactions.

Conclusions:

LAB is an innovative tool for precise interactome mapping of membrane proteins.
This technology offers improved control over proximity labeling compared to traditional methods.
LAB advances the study of membrane protein complex dynamics.