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Sigma-Aldrich

Atto 532 maleimide

BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)

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About This Item

MDL number:
UNSPSC Code:
12161900
NACRES:
NA.25

product line

BioReagent

Quality Level

Assay

≥90% (coupling to thiols)

form

powder

manufacturer/tradename

ATTO-TEC GmbH

fluorescence

λex 532 nm; λem 553 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

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


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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Toshiro Saito et al.
Nanotechnology, 22(44), 445708-445708 (2011-10-13)
We fabricated platinum bowtie nanostructure arrays producing fluorescence enhancement and evaluated their performance using two-photon photoluminescence and single-molecule fluorescence measurements. A comprehensive selection of suitable materials was explored by electromagnetic simulation and Pt was chosen as the plasmonic material for
Chunlai Chen et al.
Nucleic acids research, 35(9), 2875-2884 (2007-04-14)
Hybridization of nucleic acids with secondary structure is involved in many biological processes and technological applications. To gain more insight into its mechanism, we have investigated the kinetics of DNA hybridization/denaturation via fluorescence resonance energy transfer (FRET) on perfectly matched
STED microscopy reveals nanoparticle assemblies
Willig, K.I., et al.
New Journal of Physics, 8, 1-1 (2006)
Andrea Armbrüster et al.
FEBS letters, 579(9), 1961-1967 (2005-03-29)
The ability of subunit C of eukaryotic V-ATPases to bind ADP and ATP is demonstrated by photoaffinity labeling and fluorescence correlation spectroscopy (FCS). Quantitation of the photoaffinity and the FCS data indicate that the ATP-analogues bind more weakly to subunit
Moritz Marcinowski et al.
Nature structural & molecular biology, 18(2), 150-158 (2011-01-11)
The endoplasmic reticulum is the site of folding, assembly and quality control for proteins of the secretory pathway. The ATP-regulated Hsp70 chaperone BiP (heavy chain-binding protein), together with cochaperones, has important roles in all of these processes. The functional cycle

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