R9130
Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment antibody produced in goat
affinity isolated antibody, lyophilized powder
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About This Item
clone:
polyclonal
application:
IEP
technique(s):
immunoelectrophoresis: suitable
citations:
3
Recommended Products
biological source
goat
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
lyophilized powder
technique(s)
immunoelectrophoresis: suitable
storage temp.
2-8°C
target post-translational modification
unmodified
General description
Binds all rabbit Igs.
Application
Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment antibody produced in goat was used in fluorescence biosensor experiments.
Biochem/physiol Actions
IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections.
Physical form
Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2
Reconstitution
Reconstitute with 0.135 M sodium chloride.
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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Laurence Choulier et al.
Analytical biochemistry, 401(2), 188-195 (2010-03-02)
A ratiometric fluorescent sensor was obtained by solid-phase synthesis of a peptide singly labeled at its N-terminus with a 3-hydroxychromone (3HC) derivative, an environmentally sensitive fluorophore with a two-band emission. The construct contains the binding site recognized by an antibody
Karin Enander et al.
Bioconjugate chemistry, 19(9), 1864-1870 (2008-08-13)
We present the design, synthesis, and functional evaluation of peptide-based fluorescent constructs for wavelength-ratiometric biosensing of a protein analyte. The concept was shown using the high-affinity model interaction between the 18 amino acid peptide pTMVP and a recombinant antibody fragment
Ana María Espinosa et al.
Vaccine, 21(11-12), 1033-1043 (2003-02-01)
Among the four parasite species causing malaria in humans, Plasmodium vivax prevails on both the Asian and the American continents. Several antigens from this parasite's erythrocytic stages have been characterised and some of them are considered to be good vaccine
Kun-Chun Chiang et al.
Oncotarget, 5(11), 3849-3861 (2014-06-19)
Intrahepatic cholangiocarcinoma (ICC) is an aggressive cancer. Vitamin D, a pro-hormone, is getting popular due to its hormone-like functions after converted to its active form, 1α,25(OH)2D3. Here, we show that dietary supplementation with 6 IU/g of vitamin D greatly suppressed
A L Minella et al.
Gene therapy, 21(10), 913-920 (2014-07-25)
The cat is emerging as a promising large animal model for preclinical testing of retinal dystrophy therapies, for example, by gene therapy. However, there is a paucity of studies investigating viral vector gene transfer to the feline retina. We therefore
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