68499
Atto 532 maleimide
BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)
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About This Item
Produtos recomendados
linha de produto
BioReagent
Ensaio
≥90% (coupling to thiols)
forma
powder
fabricante/nome comercial
ATTO-TEC GmbH
fluorescência
λex 532 nm; λem 553 nm in 0.1 M phosphate pH 7.0
adequação
suitable for fluorescence
temperatura de armazenamento
−20°C
Aplicação
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.
Informações legais
This product is for Research use only. In case of intended commercialization, please contact the IP-holder (ATTO-TEC GmbH, Germany) for licensing.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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Toshiro Saito et al.
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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
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Willig, K.I., et al.
New Journal of Physics, 8, 1-1 (2006)
Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding.
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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