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80661

Sigma-Aldrich

Atto 655-maleimide

BioReagent, suitable for fluorescence, ≥90% (coupling rate)

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MDL number:
MFCD04040684
NACRES:
NA.32

product line

BioReagent

Quality Level

100

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

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Atto 565 maleimide BioReagent, suitable for fluorescence

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assay

≥90% (coupling rate)

assay

>90.0% (HPLC)

assay

≥90% (coupling to thiols)

assay

≥90% (coupling to thiols)

form

powder

form

powder

form

solid

form

-

fluorescence

λex 663 nm; λem 684 nm in 0.1 M phosphate pH 7.0

fluorescence

λex 563 nm; λem 592 nm in 0.1 M phosphate pH 7.0

fluorescence

λex 647 nm; λem 669 nm in 0.1 M phosphate pH 7.0

fluorescence

λex 645 nm; λem 715 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

suitability

-

suitability

suitable for fluorescence

suitability

suitable for fluorescence

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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

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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
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
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
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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