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74417

Sigma-Aldrich

Atto 488 amine

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

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About This Item

UNSPSC Code:
12352116
NACRES:
NA.32

product line

BioReagent

Quality Level

Assay

≥90% (HPLC)

form

solid

mol wt

Mw 858 g/mol

manufacturer/tradename

ATTO-TEC GmbH

λ

in methanol: water (1:1) (with 0.1% perchloric acid)

UV absorption

λ: 502-508 nm Amax

suitability

suitable for fluorescence

storage temp.

−20°C

General description

Atto 488 is a fluorescent label with excellent water solubility. Characteristic features of the label are strong absorption, high fluorescence quantum yield, high photostability, and very little triplet formation. Thus Atto 488 is highly suitable for single-molecule detection applications and high-resolution microscopy such as PALM, dSTORM, STED etc. Additionally the dye highly qualifies to be applied in flow cytometry (FACS), fluorescence in-situ hybridization (FISH) and many more. The fluorescence is excited most efficiently in the range 480 - 515 nm. For instance the 488 nm line of the Argon-Ion laser is very suitable for excitation.

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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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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
Jeanne C Stachowiak et al.
Nature cell biology, 14(9), 944-949 (2012-08-21)
Curved membranes are an essential feature of dynamic cellular structures, including endocytic pits, filopodia protrusions and most organelles. It has been proposed that specialized proteins induce curvature by binding to membranes through two primary mechanisms: membrane scaffolding by curved proteins
Markus Hirsch et al.
Biological chemistry, 393(1-2), 23-35 (2012-05-26)
Investigations into the fate of small interfering RNA (siRNA) after transfection may unravel new ways to improve RNA interference (RNAi) efficiency. Because intracellular degradation of RNA may prevent reliable observation of fluorescence-labeled siRNA, new tools for fluorescence microscopy are warranted

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