73353
Atto 647N iodoacetamide
BioReagent, suitable for fluorescence
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About This Item
UNSPSC Code:
12352200
product line
BioReagent
form
solid
mol wt
Mw 969 g/mol
manufacturer/tradename
ATTO-TEC GmbH
fluorescence
λex 644 nm; λem 661 nm
suitability
suitable for fluorescence
storage temp.
−20°C
General description
Atto 647N is a superior label with high molecular absorption (150.000) and quantum yield (0.65) as well as sufficient stoke′s shift. Atto 647 N 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 iodoacetamide derivative reacts, like the maleimide, with a sulfhydryl group forming a thioether bond. It is predominantly used for tagging cystein residues of proteins.
Absorption and fluorescence are independent of pH, at least in the most relevant range of pH 4 to 11. The iodoacetamide derivative reacts, like the maleimide, with a sulfhydryl group forming a thioether bond. It is predominantly used for tagging cystein residues of proteins.
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 Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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STED microscopy to monitor agglomeration of silica particles inside A549 cells.
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Advanced Engineering Materials, 12, 417-422 (2010)
A novel nanoscopic tool by combining AFM with STED microscopy.
Harke, B., et al.
Optical Nanoscopy, 1, 3-3 (2012)
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
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
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