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Related Concept Videos

Labeling DNA Probes03:31

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...
Tagging and Fusion Proteins01:24

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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...
In-situ Hybridization02:31

In-situ Hybridization

In situ hybridization (ISH) is a technique used to detect and localize specific DNA or RNA molecules in cells, tissue, or tissue sections using a labeled probe. The technique was first used in 1969 for the investigation of nucleic acids. It is currently an essential tool in scientific research and clinical settings, especially for diagnostic purposes.
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Updated: Jun 28, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

ASAP-ID: Proximity labelling with small tags.

Ruohua Lyu1, Kiersten M Ruff2, Catherine S Palmer1

  • 1Department of Biochemistry and Pharmacology and Bio21 Molecular Science and Biotechnology Institute, 30 Flemington Road. The University of Melbourne, Victoria 3010 Australia.

Molecular & Cellular Proteomics : MCP
|June 26, 2026
PubMed
Summary
This summary is machine-generated.

A new proximity labeling method, Antibody and Small-tag Assembly on Proteins for Interaction Detection (ASAP-ID), reduces steric disruption for protein interaction discovery. ASAP-ID offers flexibility and identified novel interactors for Lamin A and ALS-mutant profilin 1.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Biotinylation-based proximity labeling is crucial for identifying protein-protein interactions.
  • Current methods often require fusing target proteins with enzymes, risking disruption of native function.

Purpose of the Study:

  • To develop a proximity labeling method that minimizes steric impact and enhances flexibility.
  • To introduce Antibody and Small-tag Assembly on Proteins for Interaction Detection (ASAP-ID) for improved protein interaction studies.

Main Methods:

  • ASAP-ID utilizes a bipartite system where target proteins fuse to a peptide antigen, recruiting enzyme-fused antibodies.
  • The method was tested using SunTag and MoonTag systems for labeling human Lamin A.
  • ASAP-ID was applied in cis (ASAP-IDIC) and trans (ASAP-IDIT) configurations.

Main Results:

  • ASAP-ID successfully labeled human Lamin A in cells.
  • ASAP-IDIT identified over 448 known and novel Lamin A interactors.
  • ASAP-IDIT revealed distinct interactome changes in ALS-mutant profilin 1, correlating with aggregation propensity and cellular location.

Conclusions:

  • ASAP-ID is a versatile and less invasive tool for proximity labeling.
  • The method enables the discovery of protein interactors and the study of interactome alterations in disease models.
  • ASAP-ID provides insights into subtle differences in protein interactions and cellular localization.