R2004
Anti-Rabbit IgG (whole molecule) antibody produced in goat
affinity isolated antibody, lyophilized powder
Sinónimos:
Whole antibody
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About This Item
Productos recomendados
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
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General description
Binds all rabbit Igs.
Specificity
Anti-Rabbit IgG (whole molecule) antibody detects all rabbit Igs.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
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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Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Tianbo Sun et al.
Scientific reports, 6, 27482-27482 (2016-06-07)
A label-free optical biosensor is described that employs a silicon-based high-contrast grating (HCG) resonator with a spectral linewidth of ~500 pm that is sensitive to ligand-induced changes in surface properties. The device is used to generate thermodynamic and kinetic data
Xuefeng Wang et al.
Biosensors & bioelectronics, 26(5), 1871-1875 (2010-03-20)
Fluorescence-free biosensor arrays for protein detection directly measure the protein surface density, and do not require a fluorophore or enzyme label, and provide quantitative and consistent signals. However, few fluorescence-free biosensor protein arrays have demonstrated successful application in high-background samples
Samuel Sánchez et al.
Analytical chemistry, 80(17), 6508-6514 (2008-07-30)
The aim of this study was the fabrication and characterization of biomembranes by the phase inversion (PI) method followed by their subsequent casting onto screen-printed electrodes (SPE) for biomedical applications. The combination of multiwalled carbon nanotubes (MWCNT) as a transducer
Ishwar Gill et al.
Journal of cell science, 128(4), 768-780 (2014-12-21)
During cortical development, N-methyl-D-aspartate (NMDA) receptors (NMDARs) facilitate presynaptic terminal formation, enhance neurotransmitter release and are required in presynaptic neurons for spike-timing-dependent long-term depression (tLTD). However, the extent to which NMDARs are found within cortical presynaptic terminals has remained controversial
M P Oria et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(10), 5065-5070 (2000-05-03)
The endosperm of a sorghum mutant cultivar, with high in vitro uncooked and cooked protein digestibilities, was examined by transmission electron microscopy and alpha-, beta-, and gamma-kafirins (storage proteins) were localized within its protein bodies. Transmission electron microscopy micrographs revealed
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