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Related Experiment Video

Updated: Jul 19, 2026

ReAsH/FlAsH Labeling and Image Analysis of Tetracysteine Sensor Proteins in Cells

ReAsH/FlAsH Labeling and Image Analysis of Tetracysteine Sensor Proteins in Cells

Published on: August 31, 2011

Protein labeling with FlAsH and ReAsH.

Thomas Machleidt¹, Matt Robers, George T Hanson

¹Invitrogen Corporation, Madison, WI, USA.

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

|September 22, 2006

Summary

Fluorescent proteins (FPs) enable cell imaging but have limitations. The novel Fluorescein Arsenical Hairpin (FlAsH) technology offers a smaller, effective alternative for visualizing protein dynamics and biochemical changes in living cells.

Area of Science:

Cellular biology
Molecular imaging
Biochemistry

Background:

Imaging cellular functions in health and disease requires understanding molecular mechanisms.
Fluorescent proteins (FPs) are valuable for live-cell studies but have size and spectral limitations.

Purpose of the Study:

To introduce and demonstrate the practical application of Fluorescein Arsenical Hairpin (FlAsH) binder technology.
To showcase FlAsH as a viable alternative to FPs for protein labeling and cellular localization.

Main Methods:

Utilizing the Fluorescein Arsenical Hairpin (FlAsH)/tetracysteine binder system.
Employing a small genetically encoded peptide tag with a small molecule detection reagent.
Imaging protein dynamics in living cells.

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Main Results:

The FlAsH technology provides a promising alternative to FPs for protein labeling.
This method is suitable for investigating biochemical changes in living cells.
Successful imaging of protein dynamics was achieved using the FlAsH system.

Conclusions:

The FlAsH/tetracysteine binder technology offers advantages over FPs for specific cellular imaging applications.
This technology facilitates the study of biochemical changes and protein dynamics in living cells.
FlAsH represents a significant advancement in molecular tagging and live-cell imaging.