80661
Atto 655-maleimide
BioReagent, suitable for fluorescence, ≥90% (coupling rate)
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About This Item
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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.
Storage Class Code
11 - 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
Certificates of Analysis (COA)
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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
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
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
Søren Preus et al.
Chembiochem : a European journal of chemical biology, 13(14), 1990-2001 (2012-09-01)
Förster resonance energy transfer (FRET) is a powerful tool for monitoring molecular distances and interactions at the nanoscale level. The strong dependence of transfer efficiency on probe separation makes FRET perfectly suited for "on/off" experiments. To use FRET to obtain
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