The biarsenical dye lumiotrademark exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells

Anna Clare Hearps, Melinda J Pryor, Henna Veera Kuusisto, Stephen Matthew Rawlinson, Sabine Piller, David Andrew Jans

Research output: Contribution to journalArticleResearchpeer-review

25 Citations (Scopus)

Abstract

Investigating the localisation of proteins within live cells via fluorescence microscopy typically involves the fusion of the protein of interest to a large fluorescent protein such as green fluorescent protein (GFP). Alternate fluorescent labelling technologies such as the fluorescent biarsenical dye molecules (e.g. FlAsH, ReAsH) are preferable to the use of large fusion proteins in many respects and allow greater flexibility in terms of the location of the labelling site. We assessed the ability of the FlAsH-derived biarsenical dye molecule Lumiotrade mark to label a range of tetracysteine containing proteins within live cells and report that although in some circumstances Lumio is capable of positively detecting such proteins, the sensitivity and specificity of labelling is significantly reduced, making the Lumio-labelling system unsuitable for the detection of a wide range of protein within live cells.
Original languageEnglish
Pages (from-to)593 - 597
Number of pages5
JournalJournal of Fluorescence
Volume17
Issue number6
DOIs
Publication statusPublished - 2007

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