41051

Sigma-Aldrich

Atto 488

suitable for fluorescence, ≥90% (HPCE)

NACRES:
NA.32

Quality Level

product line

BioReagent

assay

≥90% (HPCE)

fluorescence

λex 504 nm; λem 521 nm in 0.1 M phosphate pH 7.0

suitability

suitable for fluorescence

storage temp.

−20°C

General description

Atto 488 is a labeling dye with high molecular absorption (90,000) and quantum yield (0.80) as well as sufficient Stokes shift between excitation and emission maximum. It is optimized for excitation with an argon 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 488 is suitable for preparation of fluorescence labeling reagents and the study of its physicochemical properties.

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

Silviya Zustiak et al.
Journal of biomedical optics, 17(12), 125004-125004 (2012-12-05)
Fluorescence correlation spectroscopy (FCS) is increasingly being used to assess the movement of particles diffusing in complex, optically dense surroundings, in which case measurement conditions may complicate data interpretation. It is considered how a single-photon FCS measurement can be affected...
Analysis of fluorescent nanostructures in biological systems by means of spectral position determination microscopy (SPDM).
Muller, P., et al. et al.
Current Microscopy Contributions to Advances in Science and Technology, 1, 3-12 (2012)
Monitoring single membrane protein dynamics in a liposome manipulated in solution by the ABELtrap.
Rendler, T., et al.
arXiv, 1102-1102 (2011)
Mohd A Mohd Ridzuan et al.
PloS one, 7(3), e33845-e33845 (2012-04-06)
An actomyosin motor complex assembled below the parasite's plasma membrane drives erythrocyte invasion by Plasmodium falciparum merozoites. The complex is comprised of several proteins including myosin (MyoA), myosin tail domain interacting protein (MTIP) and glideosome associated proteins (GAP) 45 and...
Tilak Jain et al.
Journal of structural biology, 179(1), 68-75 (2012-05-10)
Over the last three decades, Cryo-TEM has developed into a powerful technique for high-resolution imaging of biological macromolecules in their native vitrified state. However, the method for vitrifying specimens onto EM grids is essentially unchanged - application of ∼3 μL...

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