产品名称
Atto 655-Biotin, BioReagent, suitable for fluorescence, ≥90% (HPCE)
product line
BioReagent
assay
≥90% (HPCE)
form
powder
manufacturer/tradename
ATTO-TEC GmbH
transmittance
254 nm
655 nm
solubility
DMF: soluble
DMSO: soluble
acetonitrile: soluble
fluorescence
λex 655 nm; λem 680 nm in 0.1 M phosphate pH 7.0
λ
in ethanol (with 0.1% trifluoroacetic acid: 655 nm ± 3 nm)
suitability
suitable for fluorescence
storage temp.
−20°C
Quality Level
Application
Atto 655 conjugated to biotin is useful for binding to proteins (i.e., avidin and streptavidin). The fluorescent properties include excellent thermal and photo-stability, high quantum yield, strong absorption (663 nm) and fluorescence (684 nm), and low triplet formation. It is a zwitterionic dye, carrying a net electrical charge of zero. Electron donors such as guanine and tryptophan can easily quench the fluorescence of this fluorophore. Biotin conjugated with ATTO 655 was applied to assess efficiency of BSA/avidin structures bound to a surface.
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.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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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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
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
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
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
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