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41699

Sigma-Aldrich

Anti-Rabbit IgG−Abberior® STAR RED antibody produced in goat

for STED application

Synonym(s):

Abberior® STAR RED-Anti-Rabbit IgG antibody produced in goat

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

goat

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

rabbit

concentration

~1 mg/mL

fluorescence

λex 638 nm; λem 655 nm in PBS, pH 7.4

storage temp.

−20°C

General description

Abberior STAR RED is a well-known red dye, named also KK114 in literature. It was developed for STED and confocal imaging in the red spectral region. It shows an exceptional brightness and low background, delivering stunning STED images. The dye works extremely well with Abberior Instruments STEDYCON and Expert Line microscopes and Leica STED microscopes. Abberior STAR RED can substitute dyes like Atto 647N, Alexa Fluor 647, or Cy®5. It can be excited with lasers at wavelength between 630 - 650 nm. For STED, a depletion wavelength around 750 - 800 nm is recommended. Abberior STAR RED is the ideal partner for Abberior STAR 580 to obtain optimal 2 Color STED results. Best results are obtained with freshly prepared samples.


Photophysical properties (carboxylic acid):
Absorption Maximum, λex [nm]: 638 (PBS pH 7.4), 638 (H2O), 634 (MeOH)
Extinction Coefficient, εmax [M-1cm-1]: 120 000 (PBS pH 7.4), 125 000 (H2O), 115 000 (MeOH)
Correction Factor, CF260 = ε260max: 0,16 (PBS pH 7.4)
Correction Factor, CF280 = ε280max: 0,32 (PBS pH 7.4)
Fluorescence Maximum, λem [nm]: 655 (PBS pH 7.4), 655 (H2O), 654 (MeOH)
Recommended STED Wavelength, λ [nm]: 750-800
Fluorescence Quantum Yield, λ: 0,90 (PBS pH 7.4)
Fluorescence Lifetime, τ [ns]: 3,4 (PBS pH 7.4)

Features and Benefits

  • Unmatched, background free STED imaging cont
  • Verified in Abberior Instruments and Leica STED microscopes

Suitability

Designed and tested for fluorescent super-resolution microscopy

Analysis Note

May contain significant amounts of BSA as stabilizer
unconjugated dye ≤5% of total fluorescence

Legal Information

ALEXA FLUOR is a trademark of Life Technologies
Atto is a trademark of Atto-Tec GmbH
Cy is a registered trademark of Cytiva
abberior is a registered trademark of Abberior GmbH

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Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Céline Guilbeau-Frugier et al.
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This study explored the lateral crest structures of adult cardiomyocytes (CMs) within healthy and diseased cardiac tissue. Using high-resolution electron and atomic force microscopy, we performed an exhaustive quantitative analysis of the three-dimensional (3D) structure of the CM lateral surface
Sinem K Saka et al.
Nature communications, 5, 4509-4509 (2014-07-26)
Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter
Kirill Kolmakov et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 20(1), 146-157 (2013-12-18)
The synthesis, reactivity, and photophysical properties of new rhodamines with intense red fluorescence, two polar residues (hydroxyls, primary phosphates, or sulfonic acid groups), and improved hydrolytic stability of the amino-reactive sites (NHS esters or mixed N-succinimidyl carbonates) are reported. All
Alf Honigmann et al.
eLife, 3, e01671-e01671 (2014-03-20)
The eukaryotic cell membrane is connected to a dense actin rich cortex. We present FCS and STED experiments showing that dense membrane bound actin networks have severe influence on lipid phase separation. A minimal actin cortex was bound to a
Daniel Neumann et al.
PMC biophysics, 3(1), 4-4 (2010-03-09)
The voltage-dependent anion channel (VDAC, also known as mitochondrial porin) is the major transport channel mediating the transport of metabolites, including ATP, across the mitochondrial outer membrane. Biochemical data demonstrate the binding of the cytosolic protein hexokinase-I to VDAC, facilitating

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