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Merck
CN

77671

Anti-Rabbit IgG - Atto 594 antibody produced in goat

别名:

Atto 594 - [goat-Anti-rabbit IgG]

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NACRES:
NA.46
UNSPSC Code:
12352203
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conjugate

Atto 594 conjugate

antibody product type

secondary antibodies

clone

polyclonal

form

liquid

contains

50% glycerol as stabilizer

species reactivity

rabbit

concentration

~1 mg/mL protein

fluorescence

λex 607 nm; λem 626 nm in PBS

suitability

corresponds for gel electrophoresis

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Analysis Note

unconjugated dye ≤5% of total fluorescence; dye-to-protein ratio ≥2

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.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins. Goat anti-rabbit IgGs are known to associate with rabbit IgGs.

Legal Information

This product is for Research use only. In case of intended commercialization, please contact the IP-holder (ATTO-TEC GmbH, Germany) for licensing.

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pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Eye Irrit. 2

存储类别

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves

法规信息

常规特殊物品
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Thorsten G Müller et al.
eLife, 10 (2021-04-28)
HIV-1 replication commences inside the cone-shaped viral capsid, but timing, localization, and mechanism of uncoating are under debate. We adapted a strategy to visualize individual reverse-transcribed HIV-1 cDNA molecules and their association with viral and cellular proteins using fluorescence and
Mirko Cortese et al.
Cell host & microbe, 28(6), 853-866 (2020-11-28)
Pathogenesis induced by SARS-CoV-2 is thought to result from both an inflammation-dominated cytokine response and virus-induced cell perturbation causing cell death. Here, we employ an integrative imaging analysis to determine morphological organelle alterations induced in SARS-CoV-2-infected human lung epithelial cells.
Krzysztof Marycz et al.
International journal of nanomedicine, 16, 6049-6065 (2021-09-14)
Healing of osteoporotic defects is challenging and requires innovative approaches to elicit molecular mechanisms promoting osteoblasts-osteoclasts coupling and bone homeostasis. Cytocompatibility and biocompatibility of previously characterised nanocomposites, i.e Ca5(PO4)3OH/Fe3O4 (later called nHAp/IO) functionalised with microRNAs (nHAp/IO@miR-21/124) was tested. In vitro
Visar Ajeti et al.
Nature physics, 15, 696-705 (2020-01-04)
How cells with diverse morphologies and cytoskeletal architectures modulate their mechanical behaviors to drive robust collective motion within tissues is poorly understood. During wound repair within epithelial monolayers in vitro, cells coordinate the assembly of branched and bundled actin networks
Lena K Schroeder et al.
The Journal of cell biology, 218(1), 83-96 (2018-11-18)
The endoplasmic reticulum (ER) is composed of interconnected membrane sheets and tubules. Superresolution microscopy recently revealed densely packed, rapidly moving ER tubules mistaken for sheets by conventional light microscopy, highlighting the importance of revisiting classical views of ER structure with

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Immunoblotting (Western blot transfer) is a common technique in modern proteomics research.

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