80661
Atto 655-maleimide
BioReagent, suitable for fluorescence, ≥90% (coupling rate)
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product line
BioReagent
Quality Level
Assay
≥90% (coupling rate)
form
powder
manufacturer/tradename
ATTO-TEC GmbH
fluorescence
λex 663 nm; λem 684 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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Bengang Xing et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 17(50), 14170-14177 (2011-11-16)
The molecular interactions of the glycopeptide antibiotic vancomycin (Van) with bacterial cell wall analogues N,N'-diacetyl-L-Lys-D-Ala-D-Ala (Ac(2) KdAdA) and N,N'-diacetyl-L-Lys-D-Ala-D-Lac (Ac(2) KdAdL) were investigated in neat water, phosphate buffer and HEPES buffer by using fluorescence correlation spectroscopy (FCS) and molecular dynamics
Achim Friedrich et al.
FEBS letters, 581(8), 1644-1648 (2007-04-03)
This article presents a new, highly sensitive method for the identification of single nucleotide polymorphisms (SNPs) in homogeneous solutions using fluorescently labeled hairpin-structured oligonucleotides (smart probes) and fluorescence single-molecule spectroscopy. While the hairpin probe is closed, fluorescence intensity is quenched
Ana J García-Sáez et al.
The Journal of biological chemistry, 286(43), 37768-37777 (2011-09-03)
Pore-forming toxins have evolved to induce membrane injury by formation of pores in the target cell that alter ion homeostasis and lead to cell death. Many pore-forming toxins use cholesterol, sphingolipids, or other raft components as receptors. However, the role
Julie M G Rogers et al.
Langmuir : the ACS journal of surfaces and colloids, 27(7), 3815-3821 (2011-03-16)
The structure and function of the influenza A M2 proton channel have been the subject of intensive investigations in recent years because of their critical role in the life cycle of the influenza virus. Using a truncated version of the
Eilon Sherman et al.
Chemphyschem : a European journal of chemical physics and physical chemistry, 12(3), 696-703 (2011-01-29)
Intramolecular dynamics in the denatured state of a protein are of importance for protein folding. Native-like contact formation within the ensemble of denatured conformations of a protein may guide its transformation towards the native conformation. The efficiency of folding is
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