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HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis

Los, Georgyi V., Encell, Lance P., McDougall, Mark G., Hartzell, Danette D., Karassina, Natasha, Zimprich, Chad, Wood, Monika G., Learish, Randy, Ohana, Rachel Friedman, Urh, Marjeta, Simpson, Dan, Mendez, Jacqui, Zimmerman, Kris, Otto, Paul, Vidugiris, Gediminas, Zhu, Ji, Darzins, Aldis, Klaubert, Dieter H., Bulleit, Robert F., Wood, Keith V.·2008·ACS Chemical Biology
DOI 10.1021/cb800025k
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Abstract

We have designed a modular protein tagging system that allows different functionalities to be linked onto a single genetic fusion, either in solution, in living cells, or in chemically fixed cells. The protein tag (HaloTag) is a modified haloalkane dehalogenase designed to covalently bind to synthetic ligands (HaloTag ligands). The synthetic ligands comprise a chloroalkane linker attached to a variety of useful molecules, such as fluorescent dyes, affinity handles, or solid surfaces. Covalent bond formation between the protein tag and the chloroalkane linker is highly specific, occurs rapidly under physiological conditions, and is essentially irreversible. We demonstrate the utility of this system for cellular imaging and protein immobilization by analyzing multiple molecular processes associated with NF-kappaB-mediated cellular physiology, including imaging of subcellular protein translocation and capture of protein--protein and protein--DNA complexes.

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Crossref · 10.1021/cb800025k

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  • Dendra2 has properties including a monomeric state, low phototoxic activation and efficient chromophore maturation, which make it suitable for real-time tracking of LC3 and SQSTM1.

    “This modified version of the fluorophore has certain properties including a monomeric state, low phototoxic activation and efficient chromophore maturation, which make it suitable for real-time tracking of LC3 and SQSTM1 (Figure 13; [361]).”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [361]

  • SQSTM1 expression can be positively regulated post-transcriptionally by ELAVL1/HuR protein which binds to SQSTM1 transcript in ARPE19 cells exposed to 24-h MG132 treatment.

    “SQSTM1 expression can be positively regulated post-transcriptionally by the ELAVL1/HuR protein which binds to the SQSTM1 transcript in ARPE19 cells exposed to 24-h MG132 treatment [361].”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [361]

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Metadata

Authors
Los, G. V., Encell, L. P., McDougall, M. G., Hartzell, D. D., Karassina, N., Zimprich, C., Wood, M. G., Learish, R., Ohana, R. F., Urh, M., Simpson, D., Mendez, J., Zimmerman, K., Otto, P., Vidugiris, G., Zhu, J., Darzins, A., Klaubert, D. H., Bulleit, R. F., & Wood, K. V.
Affiliations
  • Promega Corporation, 2800 Woods Hollow Rd., Madison, Wisconsin 53711
  • Promega Biosciences Incorporated, 277 Granada Dr., San Luis Obispo, California 93401
Venue
ACS Chemical Biology
Publisher
American Chemical Society (ACS)
Published
2008-06-01
Volume
3
Issue
6
Pages
373-382
ISSN
  • 1554-8929
  • 1554-8937
DOI
10.1021/cb800025k
Cited by
2,624
References
0
Language
en

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