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Merck
모든 사진(1)

문서

91000

Sigma-Aldrich

Atto 647N azide

BioReagent, suitable for fluorescence

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About This Item

UNSPSC 코드:
12352125
NACRES:
NA.32

제품 라인

BioReagent

형태

solid

분자량

Mw 959 g/mol

제조업체/상표

ATTO-TEC GmbH

형광

λex 644 nm; λem 661 nm

적합성

suitable for fluorescence

저장 온도

−20°C

관련 카테고리

일반 설명

Atto 647N is a superior red-emitting label with high molecular absorption (150.000) and quantum yield (0.65) as well as sufficient stoke′s shift. Atto 647N is characterized by a high thermal and photostability. Absorption and fluorescence are independent of pH, at least in the most relevant range of pH 4 to 11. The azide modification is suitable for reactions with alkyne groups (Huisgen reaction - "Click Chemistry").

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리 방문

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
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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