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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...
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...

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Updated: Jul 6, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

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Telomerase catalyzed fluorescent probes for sensitive protein profiling based on one-dimensional microfluidic beads

Jianhui Wen1, Xiaohai Yang, Kemin Wang

  • 1State Key Laboratory of Chemo, Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Biomedical Engineering Center, Hunan University, Changsha 410082, China.

Biosensors & Bioelectronics
|April 5, 2008
PubMed
Summary

This study introduces a novel nucleic acid method for detecting multiple proteins using telomerase-catalyzed fluorescent probes. This highly sensitive assay offers a simple, fast, and cost-effective approach for analyzing cellular protein expression, aiding cancer research.

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Last Updated: Jul 6, 2026

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Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
10:49

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Assay Development

Background:

  • Accurate detection of multiple proteins is crucial for understanding cellular processes and disease progression.
  • Existing methods for protein detection can be complex, time-consuming, and lack sensitivity for low-abundance targets.

Purpose of the Study:

  • To develop a sensitive and efficient nucleic acid-based signal amplification method for multiplexed protein detection.
  • To utilize telomerase-catalyzed fluorescent probes for enhanced signal generation in a one-dimensional beads array.

Main Methods:

  • Synthesis of biotin-labeled fluorescent probes with high fluorescein incorporation using telomerase.
  • Development of a one-dimensional beads array for simultaneous detection of multiple proteins.
  • Application of the assay for quantifying p53 protein and analyzing expression changes of p53, c-myc, and beta-actin in CNE2 cells.

Main Results:

  • Achieved a low limit of detection for p53 protein at 1.1 pM with a 3-order linear dynamic range.
  • Demonstrated sensitivity nearly two orders higher than traditional sandwich immunoassays.
  • Successfully determined cellular p53 levels and monitored expression changes in response to anti-cancer drugs.

Conclusions:

  • The developed method is simple, fast, cheap, and suitable for multi-protein analysis.
  • Offers significant advantages over immuno-polymerase chain reaction and immuno-rolling circle amplification.
  • Provides new opportunities for fundamental research in tumor development, particularly for low-abundance protein analysis.