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Merck

68499

Sigma-Aldrich

Atto 532 maleimide

BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)

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About This Item

MDL number:
UNSPSC Code:
12161900
NACRES:
NA.25

product line

BioReagent

assay

≥90% (coupling to thiols)

form

powder

manufacturer/tradename

ATTO-TEC GmbH

fluorescence

λex 532 nm; λem 553 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

storage temp.

−20°C

Application

Atto fluorescent labels are designed for high sensitivity applications, including single molecule detection. Atto labels have rigid structures that do not show any cis-trans-isomerization. Thus these labels display exceptional intensity with minimal spectral shift on conjugation.

Legal Information

This product is for Research use only. In case of intended commercialization, please contact the IP-holder (ATTO-TEC GmbH, Germany) for licensing.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Toshiro Saito et al.
Nanotechnology, 22(44), 445708-445708 (2011-10-13)
We fabricated platinum bowtie nanostructure arrays producing fluorescence enhancement and evaluated their performance using two-photon photoluminescence and single-molecule fluorescence measurements. A comprehensive selection of suitable materials was explored by electromagnetic simulation and Pt was chosen as the plasmonic material for
Chunlai Chen et al.
Nucleic acids research, 35(9), 2875-2884 (2007-04-14)
Hybridization of nucleic acids with secondary structure is involved in many biological processes and technological applications. To gain more insight into its mechanism, we have investigated the kinetics of DNA hybridization/denaturation via fluorescence resonance energy transfer (FRET) on perfectly matched
STED microscopy reveals nanoparticle assemblies
Willig, K.I., et al.
New Journal of Physics, 8, 1-1 (2006)
Andrea Armbrüster et al.
FEBS letters, 579(9), 1961-1967 (2005-03-29)
The ability of subunit C of eukaryotic V-ATPases to bind ADP and ATP is demonstrated by photoaffinity labeling and fluorescence correlation spectroscopy (FCS). Quantitation of the photoaffinity and the FCS data indicate that the ATP-analogues bind more weakly to subunit
Roland Bienert et al.
Chemphyschem : a European journal of chemical physics and physical chemistry, 12(3), 510-517 (2011-02-03)
H(+)-ATP synthases are molecular machines which couple transmembrane proton transport with ATP synthesis from ADP and inorganic phosphate by a rotational mechanism. Single-pair fluorescence resonance energy transfer (spFRET) in single molecules is a powerful tool to analyse conformational changes. It

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