40839
Anti-Rabbit-IgG - Atto 647N antibody produced in goat
1 mg/mL IgG
Synonym(s):
Atto 647N-Anti-Rabbit-IgG antibody produced in goat
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About This Item
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
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
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.
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.
Analysis Note
unconjugated dye ≤5% of total fluorescence
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.
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.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Till F M Andlauer et al.
eLife, 3 (2014-11-14)
CIDE-N domains mediate interactions between the DNase Dff40/CAD and its inhibitor Dff45/ICAD. In this study, we report that the CIDE-N protein Drep-2 is a novel synaptic protein important for learning and behavioral adaptation. Drep-2 was found at synapses throughout the
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 Albisetti et al.
PLoS pathogens, 13(11), e1006710-e1006710 (2017-11-02)
Trypanosoma brucei belongs to a group of unicellular, flagellated parasites that are responsible for human African trypanosomiasis. An essential aspect of parasite pathogenicity is cytoskeleton remodelling, which occurs during the life cycle of the parasite and is accompanied by major
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
Intracellular repair of oxidation-damaged α-synuclein fails to target C-terminal modification sites.
Andres Binolfi et al.
Nature communications, 7, 10251-10251 (2016-01-26)
Cellular oxidative stress serves as a common denominator in many neurodegenerative disorders, including Parkinson's disease. Here we use in-cell NMR spectroscopy to study the fate of the oxidation-damaged Parkinson's disease protein alpha-synuclein (α-Syn) in non-neuronal and neuronal mammalian cells. Specifically
Articles
Immunoblotting (Western blot transfer) is a common technique in modern proteomics research.
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