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Merck

05316

Supelco

Atto 647N马来酰亚胺

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

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About This Item

MDL號碼:
分類程式碼代碼:
12352111
NACRES:
NA.32

產品線

BioReagent

品質等級

化驗

≥90% (HPLC)
≥90% (degree of coupling)

製造商/商標名

ATTO-TEC GmbH

&lambda ;

in ethanol (with 0.1% trifluoroacetic acid)

紫外吸收

λ: 640-646 nm Amax

適合性

suitable for fluorescence

檢測方法

fluorometric

儲存溫度

−20°C

應用


  • Preparation of homogeneous samples of double-labelled protein suitable for single-molecule FRET measurements.: This study explores the use of Atto 647N maleimide for the preparation of homogeneously double-labelled protein samples, facilitating precise single-molecule FRET measurements to analyze protein dynamics and interactions (Lerner et al., 2013).

法律資訊

本产品仅供研究使用。如果打算商业化,请联系知识产权持有者(德国ATTO-TEC GmbH公司)申请许可。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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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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