06699

Sigma-Aldrich

Atto 532

BioReagent, suitable for fluorescence, ≥90% (HPCE)

MDL number:
NACRES:
NA.25
Pricing and availability is not currently available.

Quality Level

product line

BioReagent

assay

≥90% (HPCE)

fluorescence

λex 533 nm; λem 560 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

storage temp.

−20°C

General description

Atto 532 is a new label with high molecular absorption (115,000) and quantum yield (0.90) as well as sufficient Stoke′s shift between excitation and emission maximum. It is optimized for excitation with frequency doubled Nd:YAG-Laser, and is characterized by high photostability.

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 532 has been conjugated with the secondary antibodies for STED (stimulated emission depletion) microscopy and immunofluorescence studies.

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

3D reconstruction of high-resolution STED microscope images.
Punge A et al.
Microscopy Research and Technique, 71, 644-644 (2008)
Uffe V Schneider et al.
BMC biotechnology, 10, 4-4 (2010-01-28)
Melting temperature of DNA structures can be determined on the LightCycler using quenching of FAM. This method is very suitable for pH independent melting point (Tm) determination performed at basic or neutral pH, as a high throughput alternative to UV...
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...
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...
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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