Product Name
Anti-Rabbit-IgG - Atto 647N antibody produced in goat, 1 mg/mL IgG
conjugate
Atto 647N conjugate
antibody product type
secondary antibodies
clone
polyclonal
form
liquid
contains
50% glycerol as stabilizer
species reactivity
rabbit
concentration
1 mg/mL IgG
technique(s)
immunofluorescence: suitable (5μg/ml)
fluorescence
λex 647 nm; λem 665 nm in PBS
suitability
in accordance for fluorescence
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Related Categories
Analysis Note
unconjugated dye ≤5% of total fluorescence
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunofluorescence (1 paper)
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.Atto 647N goat anti-rabbit IgG was used as the secondary antibody for immunofluorescene at a concentration of 5μg/ml on cells fixed in 2% formaldehyde.
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.
Immunogen
rabbit IgG
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.
Physical form
Atto 647 goat anti-rabbit IgG (whole molecule) is provided in unit sizes of 1 ml as 1 mg/ml solution in 0.1 M sodium phosphate, 0.1 M NaCl, pH 7.5, containing 5 mM sodium azide as a preservative.
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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Masfique Mehedi et al.
Bio-protocol, 7(17) (2017-10-24)
Human respiratory syncytial virus (RSV) infection in human lung epithelial A549 cells induces filopodia, cellular protrusions consisting of F-actin, that extend to neighboring uninfected cells (Mehedi et al., 2016). High-resolution imaging via stimulated emission depletion (STED) microscopy revealed filamentous RSV
Yoori Kim et al.
Nucleic acids research, 47(4), 1823-1835 (2018-12-13)
Intrinsically disordered regions (IDRs) are present in at least 30% of the eukaryotic proteome and are enriched in chromatin-associated proteins. Using a combination of genetics, biochemistry and single-molecule biophysics, we characterize how IDRs regulate the functions of the yeast MutLα
Janin Lautenschläger et al.
Nature communications, 9(1), 712-712 (2018-02-21)
Alpha-synuclein is known to bind to small unilamellar vesicles (SUVs) via its N terminus, which forms an amphipathic alpha-helix upon membrane interaction. Here we show that calcium binds to the C terminus of alpha-synuclein, therewith increasing its lipid-binding capacity. Using
Giuliana Fusco et al.
Nature communications, 7, 12563-12563 (2016-09-20)
α-synuclein (αS) is an intrinsically disordered protein whose fibrillar aggregates are the major constituents of Lewy bodies in Parkinson's disease. Although the specific function of αS is still unclear, a general consensus is forming that it has a key role
Anna M Chizhik et al.
Molecular biology of the cell (2018-02-16)
We report a novel method, dual color axial nanometric localization by Metal Induced Energy Transfer (dcMIET), and combine it with Förster Resonant Energy Transfer (FRET) for resolving structural details in cells on the molecular level. We demonstrate the capability of
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