Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 593 - 597 |
| Number of pages | 5 |
| Journal | Journal of Fluorescence |
| Volume | 17 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2007 |
Cite this
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The biarsenical dye lumiotrademark exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells. / Hearps, Anna Clare; Pryor, Melinda J; Kuusisto, Henna Veera; Rawlinson, Stephen Matthew; Piller, Sabine; Jans, David Andrew.
In: Journal of Fluorescence, Vol. 17, No. 6, 2007, p. 593 - 597.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - The biarsenical dye lumiotrademark exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells
AU - Hearps, Anna Clare
AU - Pryor, Melinda J
AU - Kuusisto, Henna Veera
AU - Rawlinson, Stephen Matthew
AU - Piller, Sabine
AU - Jans, David Andrew
PY - 2007
Y1 - 2007
N2 - 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.
AB - 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.
UR - http://www.scopus.com/record/display.url?eid=2-s2.0-35948932520&origin=inward&txGid=wpKO6atOD83PI4Fscozu943%3a22
U2 - 10.1007/s10895-007-0225-x
DO - 10.1007/s10895-007-0225-x
M3 - Article
VL - 17
SP - 593
EP - 597
JO - Journal of Fluorescence
JF - Journal of Fluorescence
SN - 1053-0509
IS - 6
ER -