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93606

Sigma-Aldrich

Atto 647N-Biotin

BioReagent, suitable for fluorescence, ≥90.0% (HPLC)

Synonym(s):

Biotin-Atto 647N

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About This Item

UNSPSC Code:
12161900
NACRES:
NA.25

product line

BioReagent

Assay

≥90.0% (HPLC)

form

powder

manufacturer/tradename

ATTO-TEC GmbH

λ

in ethanol (with 0.1% trifluoroacetic acid)

UV absorption

λ: 642.0-648.0 nm Amax

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.

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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STED microscopy to monitor agglomeration of silica particles inside A549 cells.
Schubbe, S., et al.
Advanced Engineering Materials, 12, 417-422 (2010)
Marina I Giannotti et al.
Biomacromolecules, 12(7), 2524-2533 (2011-05-25)
Nanopharmaceutics composed of a carrier and a protein have the potential to improve the activity of therapeutical proteins. Therapy for lysosomal diseases is limited by the lack of effective protein delivery systems that allow the controlled release of specific proteins
Harpreet Singh et al.
Mitochondrion, 12(2), 230-236 (2011-10-11)
The visualization and quantification of mitochondria-associated proteins with high power microscopy methods is of particular interest to investigate protein architecture in this organelle. We report the usage of a custom-made STimulated Emission Depletion (STED) fluorescence nanoscope with ~30nm lateral resolution
S E D Webb et al.
Optics express, 16(25), 20258-20265 (2008-12-10)
We combine single molecule fluorescence orientation imaging with single-pair fluorescence resonance energy transfer microscopy, using a total internal reflection microscope. We show how angles and FRET efficiencies can be determined for membrane proteins at the single molecule level and provide
Marisa L Martin-Fernandez et al.
International journal of molecular sciences, 13(11), 14742-14765 (2012-12-04)
Insights from single-molecule tracking in mammalian cells have the potential to greatly contribute to our understanding of the dynamic behavior of many protein families and networks which are key therapeutic targets of the pharmaceutical industry. This is particularly so at

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