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Merck
CN

05316

Supelco

Atto 647N马来酰亚胺

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

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About This Item

MDL编号:
UNSPSC代码:
12352111
NACRES:
NA.32

产品线

BioReagent

质量水平

方案

≥90% (HPLC)
≥90% (degree of coupling)

制造商/商品名称

ATTO-TEC GmbH

λ

in ethanol (with 0.1% trifluoroacetic acid)

紫外吸收

λ: 640-646 nm Amax

适用性

suitable for fluorescence

检测方法

fluorometric

储存温度

−20°C

应用


  • 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).

法律信息

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。

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储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


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分析证书(COA)

Lot/Batch Number

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访问文档库

A novel nanoscopic tool by combining AFM with STED microscopy.
Harke, B., et al.
Optical Nanoscopy, 1, 3-3 (2012)
STED microscopy to monitor agglomeration of silica particles inside A549 cells.
Schubbe, S., et al.
Advanced Engineering Materials, 12, 417-422 (2010)
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
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
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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