06966

Sigma-Aldrich

Atto 655-Biotin

BioReagent, suitable for fluorescence, ≥95.0% (HPCE)

Synonym(s):
Biotin-Atto 655
NACRES:
NA.32

Quality Level

product line

BioReagent

assay

≥95.0% (HPCE)

solubility

DMF: soluble
DMSO: soluble
acetonitrile: soluble

fluorescence

λex 655 nm; λem 680 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

storage temp.

−20°C

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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...
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...
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...
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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