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R1131

Sigma-Aldrich

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

whole antiserum

Synonym(s):

Goat Anti-Rabbit IgG (whole molecule)

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About This Item

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

biological source

goat

Quality Level

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

secondary antibodies

clone

polyclonal

contains

15 mM sodium azide

technique(s)

indirect ELISA: 1:150,000
quantitative precipitin assay: 15.0 mg/mL

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Anti-Rabbit IgG is developed in goat using rabbit IgG isolated from normal rabbit serum as the immunogen. IgG is present in large quantities in the human serum. It constitutes about 10-20% of the plasma proteins. IgG is composed of glycoproteins, out of which it is 82-96% proteins and 4-18% carbohydrates. It consists of four sub-classes i.e IgG1, IgG2, IgG3, and IgG4. IgG is composed of four polypeptide chains-two heavy chains (γchains) and two light chains (κ or λ chains) which are linked by inter-chain disulfide bonds. The heavy chains consist of a N-terminal variable domain (VH) and three constant domains (CH1, CH2, CH3). A hinge region exists between the CH1 and CH2 region. The light chains have one N-terminal variable domain (VL) and one constant domain (CL). The heavy and the light chains are linked at VH and CH1 domain to form the Fab arm (Fragment antigen binding). The antigen binds to the V regions of the antibody.

Application

Anti-Rabbit IgG (whole molecule) antibody produced in goat was used for immunohistochemistry of rat brain sections. It was also used in protein spotting assays.

Biochem/physiol Actions

IgG 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.

Preparation Note

treated to remove lipoproteins

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

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Jian Han et al.
The Journal of nutrition, 132(9), 2769-2774 (2002-09-11)
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Jeongsik Yong et al.
The EMBO journal, 21(5), 1188-1196 (2002-02-28)
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Emre Ozkumur et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(23), 7988-7992 (2008-06-05)
Direct monitoring of primary molecular-binding interactions without the need for secondary reactants would markedly simplify and expand applications of high-throughput label-free detection methods. A simple interferometric technique is presented that monitors the optical phase difference resulting from accumulated biomolecular mass.
Chulmin Joo et al.
Biosensors & bioelectronics, 25(2), 275-281 (2009-08-14)
Quantitative measurement of affinities and kinetics of various biomolecular interactions such as protein-protein, protein-DNA and receptor-ligand is central to our understanding of basic molecular and cellular functions and is useful for therapeutic evaluation. Here, we describe a laser-scanning quantitative imaging

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