61967
Chromeo™ 642-Azid
for click labeling
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About This Item
UNSPSC-Code:
12352202
NACRES:
NA.32
Empfohlene Produkte
Form
solid
Löslichkeit
DMF: 0.5 mg/mL, clear, blue
Fluoreszenz
λex 646 nm±5 nm; λem 666 nm±5 nm in PBS, pH 7.4
Lagertemp.
−20°C
Allgemeine Beschreibung
C38H52N6O4P(Br) MW 687 (767 inkl. Br- -Anion)
Anwendung
Reactive fluorescent Chromeo Dyes serve as bright labels for antibodies and other biomolecules, enabling detection in immunofluorescence, high content screening, ELISA, FRET applications or flow cytometry. Chromeo 642 may be used in place of Cy5 dye. Chromeo 642-Azide is provided for click labeling applications.
Rechtliche Hinweise
Chromeo is a trademark of Active Motif Chromeon GmbH
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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Lei Chen et al.
The Journal of organic chemistry, 73(21), 8279-8285 (2008-10-02)
In search of an appropriate position for the fluorescent labeling, six chemically available positions of the flavonone core of naringenin have been examined. A number of azido-containing naringenin derivatives were accordingly prepared in various site-specific fashions, and the mild Cu(I)-catalyzed
Ziyang Hao et al.
Chemical communications (Cambridge, England), 47(15), 4502-4504 (2011-03-10)
A concise route was developed for the facile synthesis of a cyclic pyrrolysine analogue bearing an azide handle. Directed evolution enabled the encoding of this non-natural amino acid in both prokaryotic and eukaryotic cells, which offers a highly efficient approach
Yuri Motorin et al.
Nucleic acids research, 39(5), 1943-1952 (2010-11-03)
This work identifies the combination of enzymatic transfer and click labeling as an efficient method for the site-specific tagging of RNA molecules for biophysical studies. A double-activated analog of the ubiquitous co-substrate S-adenosyl-l-methionine was employed to enzymatically transfer a five
Migle Tomkuviene et al.
Nucleic acids research, 40(14), 6765-6773 (2012-05-09)
Biophysical and mechanistic investigation of RNA function requires site-specific incorporation of spectroscopic and chemical probes, which is difficult to achieve using current technologies. We have in vitro reconstituted a functional box C/D small ribonucleoprotein RNA 2'-O-methyltransferase (C/D RNP) from the
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