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Merck
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Key Documents

R2004

Sigma-Aldrich

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

affinity isolated antibody, lyophilized powder

Synonyme(s) :

Whole antibody

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

goat

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

lyophilized powder

Technique(s)

immunoelectrophoresis: suitable

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

Binds all rabbit Igs.

Spécificité

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)

Actions biochimiques/physiologiques

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.

Forme physique

Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2

Reconstitution

Reconstitute with 0.135 M sodium chloride.

Clause de non-responsabilité

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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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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