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93606

Sigma-Aldrich

Atto 647N-Biotin

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

Sinónimos:

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «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)
A novel nanoscopic tool by combining AFM with STED microscopy.
Harke, B., et al.
Optical Nanoscopy, 1, 3-3 (2012)
Volker Westphal et al.
Science (New York, N.Y.), 320(5873), 246-249 (2008-02-23)
We present video-rate (28 frames per second) far-field optical imaging with a focal spot size of 62 nanometers in living cells. Fluorescently labeled synaptic vesicles inside the axons of cultured neurons were recorded with stimulated emission depletion (STED) microscopy in
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
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
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