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Sigma-Aldrich

Atto 565

BioReagent, suitable for fluorescence

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About This Item

Empirical Formula (Hill Notation):
C31H31ClN2O9
Molecular Weight:
611.04
MDL number:
MFCD03456130
UNSPSC Code:
12352108
NACRES:
NA.32

product line

BioReagent

Quality Level

100

Assay

≥90.0% (HPLC)

form

powder

manufacturer/tradename

ATTO-TEC GmbH

λ

in ethanol (with 0.1% trifluoroacetic acid)

UV absorption

λ: 562.0-568.0 nm Amax

suitability

suitable for fluorescence

storage temp.

−20°C

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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.
Atto 565 shows a molar extinction of 120.000 and QY of 92% in water (97% in ethanol). Decay time is 3.4 ns.
Specific and stable fluorescence labeling of histidine-tagged proteins

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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06699

Atto 532

Suman Lata et al.
Journal of the American Chemical Society, 128(7), 2365-2372 (2006-02-16)
Labeling of proteins with fluorescent dyes offers powerful means for monitoring protein interactions in vitro and in live cells. Only a few techniques for noncovalent fluorescence labeling with well-defined localization of the attached dye are currently available. Here, we present
Takao Nakata et al.
The Journal of cell biology, 194(2), 245-255 (2011-07-20)
Polarized transport in neurons is fundamental for the formation of neuronal circuitry. A motor domain-containing truncated KIF5 (a kinesin-1) recognizes axonal microtubules, which are enriched in EB1 binding sites, and selectively accumulates at the tips of axons. However, it remains
Łukasz Krzemiński et al.
Journal of the American Chemical Society, 133(38), 15085-15093 (2011-08-26)
A combined fluorescence and electrochemical method is described that is used to simultaneously monitor the type-1 copper oxidation state and the nitrite turnover rate of a nitrite reductase (NiR) from Alcaligenes faecalis S-6. The catalytic activity of NiR is measured
Marie-Luise Humpert et al.
Proteomics, 12(12), 1938-1948 (2012-05-25)
PTMs of extracellular domains of membrane proteins can influence antibody binding and give rise to ambivalent results. Best proof of protein expression is the use of complementary methods to provide unequivocal evidence. CXCR7, a member of the atypical chemokine receptor
Sebastian van de Linde et al.
Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 8(4), 465-469 (2009-04-02)
We introduce a general approach for multicolor subdiffraction-resolution fluorescence imaging based on photoswitching of standard organic fluorophores. Photoswitching of ordinary fluorophores such as ATTO520, ATTO565, ATTO655, ATTO680, or ATTO700, i.e. the reversible transition from a fluorescent to a nonfluorescent state
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