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Key Documents

R2004

Sigma-Aldrich

Anti-Rabbit IgG (whole molecule) antibody produced in goat

affinity isolated antibody, lyophilized powder

Synonym(s):

Whole antibody

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

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)

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 Code

11 - Combustible Solids

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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