68499
Atto 532 maleimide
BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)
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About This Item
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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)
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Kiyoto Kamagata et al.
Journal of the American Chemical Society, 134(28), 11525-11532 (2012-06-14)
A method was developed to detect fluorescence intensity signals from single molecules diffusing freely in a capillary cell. A unique optical system based on a spherical mirror was designed to enable quantitative detection of the fluorescence intensity. Furthermore, "flow-and-stop" control
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
John F Lesoine et al.
Nano letters, 12(6), 3273-3278 (2012-06-06)
We present a method for measuring the fluorescence from a single molecule hundreds of times without surface immobilization. The approach is based on the use of electroosmosis to repeatedly drive a single target molecule in a fused silica nanochannel through
Daniel Aquino et al.
Nature methods, 8(4), 353-359 (2011-03-15)
We demonstrate three-dimensional (3D) super-resolution imaging of stochastically switched fluorophores distributed across whole cells. By evaluating the higher moments of the diffraction spot provided by a 4Pi detection scheme, single markers can be simultaneously localized with <10 nm precision in
Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding.
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
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