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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

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...

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Related Experiment Video

Updated: May 28, 2026

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis
07:44

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

Spatiotemporally Resolved Protein Tagging for Dynamic and Tissue-Specific Secretome Profiling In Vivo.

Qizhen Zheng1,2, Rui Yao1,2, Tianyu Ma1,2

  • 1Beijing National Laboratory For Molecular Sciences, CAS Key Laboratory of Analytical Chemistry For Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences, Beijing, China.

Angewandte Chemie (International Ed. in English)
|May 26, 2026
PubMed
Summary

Researchers developed STePTag, a new tool for tracking secreted proteins in live animals. This method precisely maps the secretome, identifying key proteins involved in liver injury and repair.

Keywords:
Proximity LabelingSecretomeSpatiotemporalTissue‐specific lipid nanoparticlesTurboID

More Related Videos

Inducible LAP-tagged Stable Cell Lines for Investigating Protein Function, Spatiotemporal Localization and Protein Interaction Networks
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Inducible LAP-tagged Stable Cell Lines for Investigating Protein Function, Spatiotemporal Localization and Protein Interaction Networks

Published on: December 24, 2016

Related Experiment Videos

Last Updated: May 28, 2026

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis
07:44

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

Inducible LAP-tagged Stable Cell Lines for Investigating Protein Function, Spatiotemporal Localization and Protein Interaction Networks
11:04

Inducible LAP-tagged Stable Cell Lines for Investigating Protein Function, Spatiotemporal Localization and Protein Interaction Networks

Published on: December 24, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein secretion is vital for physiological and pathological processes.
  • Existing methods lack spatial and temporal resolution for in vivo secretome profiling.

Purpose of the Study:

  • To develop a novel system for spatiotemporally resolved secretome profiling in live animals.
  • To identify liver-secreted proteins and their dynamic regulation during acute liver injury.

Main Methods:

  • Introduced STePTag (Spatio-Temporal Protein Tagging), a conditional proximity labeling system.
  • Utilized TurboID enzyme and dihydrofolate reductase (DHFR) domain with trimethoprim (TMP) for controlled labeling.
  • Employed tissue-specific lipid nanoparticles (tsLNPs) for targeted delivery to the mouse liver.
  • Confined labeling to the secretory pathway by targeting STePTag to the endoplasmic reticulum (ER).

Main Results:

  • Identified 93 liver-derived secretory proteins under physiological conditions.
  • Discovered 40 dynamically regulated proteins in an acetaminophen-induced acute liver injury (ALI) model.
  • Functionally validated Aldh1a1 as a protective factor in ALI.

Conclusions:

  • STePTag offers a versatile platform for in vivo secretome analysis with high spatial and temporal resolution.
  • Enables discovery of context-dependent biomarkers and tissue-derived signaling molecules.
  • Provides insights into protein secretion dynamics in native physiological and pathological environments.