80661
Atto 655-maleimide
BioReagent, suitable for fluorescence, ≥90% (coupling rate)
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About This Item
Produtos recomendados
linha de produto
BioReagent
Nível de qualidade
Ensaio
≥90% (coupling rate)
Formulário
powder
fabricante/nome comercial
ATTO-TEC GmbH
fluorescência
λex 663 nm; λem 684 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.
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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
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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
The journal of physical chemistry. B, 115(17), 5001-5007 (2011-04-12)
Atto655 has been widely used as an excellent probing dye through photoinduced electron transfer (PET) for biochemical processes in oligonucleotides or polypeptides. However, its photophysical properties in the presence of the quenchers guanosine and tryptophan have not been carefully studied.
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
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
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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