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95349

Sigma-Aldrich

Atto 647N amine

BioReagent, suitable for fluorescence

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About This Item

Code UNSPSC :
12352116
Nomenclature NACRES :
NA.32

Gamme de produits

BioReagent

Pureté

≥90% (HPLC)

Forme

solid

Poids mol.

Mw 801 g/mol

Fabricant/nom de marque

ATTO-TEC GmbH

λ

in ethanol (with 0.1% trifluoroacetic acid)

Absorption UV

λ: 640-646 nm Amax

Adéquation

suitable for fluorescence

Température de stockage

−20°C

Description générale

Atto 647N is a superior red-emitting label with high molecular absorption (150.000) and quantum yield (0.65) as well as sufficient stoke′s shift. Atto 647N is characterized by a high thermal and photostability.
Absorption and fluorescence are independent of pH, at least in the most relevant range of pH 4 to 11. The amine derivative may be used for reactions with activated carboxy-groups like NHS-esters, TFP-esters etc.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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STED microscopy to monitor agglomeration of silica particles inside A549 cells.
Schubbe, S., et al.
Advanced Engineering Materials, 12, 417-422 (2010)
Marina I Giannotti et al.
Biomacromolecules, 12(7), 2524-2533 (2011-05-25)
Nanopharmaceutics composed of a carrier and a protein have the potential to improve the activity of therapeutical proteins. Therapy for lysosomal diseases is limited by the lack of effective protein delivery systems that allow the controlled release of specific proteins
Harpreet Singh et al.
Mitochondrion, 12(2), 230-236 (2011-10-11)
The visualization and quantification of mitochondria-associated proteins with high power microscopy methods is of particular interest to investigate protein architecture in this organelle. We report the usage of a custom-made STimulated Emission Depletion (STED) fluorescence nanoscope with ~30nm lateral resolution
S E D Webb et al.
Optics express, 16(25), 20258-20265 (2008-12-10)
We combine single molecule fluorescence orientation imaging with single-pair fluorescence resonance energy transfer microscopy, using a total internal reflection microscope. We show how angles and FRET efficiencies can be determined for membrane proteins at the single molecule level and provide
Marisa L Martin-Fernandez et al.
International journal of molecular sciences, 13(11), 14742-14765 (2012-12-04)
Insights from single-molecule tracking in mammalian cells have the potential to greatly contribute to our understanding of the dynamic behavior of many protein families and networks which are key therapeutic targets of the pharmaceutical industry. This is particularly so at
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