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I5260

Sigma-Aldrich

Anti-Human IgG (Fab specific) antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Fab-Specific Antibody

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.46

Origine biologica

goat

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

secondary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

tecniche

indirect ELISA: 1:50,000
quantitative precipitin assay: 2.0 mg/mL

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

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Categorie correlate

Descrizione generale

Anti-Human IgG (Fab specific) antiserum is produced in goat using purified human IgG Fab fragment as the immunogen. Affinity isolated antibody is obtained from goat anti-human IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fab fragment of human IgG. IgG is a larger molecule with a molecular weight of 150 kilo daltons (kDa). IgG has two light chains (L) and two heavy chains (H). The light chain can be either lambda (λ) or kappa (κ) chain. Functionally, immunoglobulins have constant region and variable region. Light chain has one variable region in the N-terminal VL and followed by one constant domain CL. The light chain is approximately about 25 kDa. The heavy chain has one variable region in the N-terminal and followed by three constant domains. In between the first (C1H) and second constant (C2H) domain in the spacer hinge region which connects both the heavy chains. Each heavy chain is about 55 kDa.

Specificità

Goat anti-human IgG (Fab specific) antibody reacts specifically with Fab fragment of human IgG and shows no reactivity for Fc fragment of human IgG. This product has no interspecies cross reactivity for mouse and rat IgG.

Immunogeno

Purified human IgG Fab fragment.

Applicazioni

Anti-Human IgG (Fab specific) antibody produced in goat is effective as a second antibody reagent in immunoassay procedures. It may be used:
  • as starting material for conjugates using enzymes or fluorescent dyes
  • in enzyme linked immunosorbent assay
  • as a cross-linking antibody in internalisation of 125I-IgG by streptolysin-O-permeabilised cells
  • as capture antibody in enzyme-linked immunosorbent assay (ELISA) for detection and semiquantitation of Fab
  • in electrophoresis and immunoelectrophoresis

Azioni biochim/fisiol

Enzymatic cleavage of IgG yields antigen-binding (Fab) and effector activating (Fc) fragments. IgG treatment with papain produces two Fab fragments and one Fc fragment. IgG treatment with pepsin produces (Fab′)2 fragment alone. IgG antibodies regulate several functions such as complement activation and phagocytosis. Thus they play a crucial role in facilitating cytological immune responses. Anti-human IgG (Fab specific) antibody can be used in Ouchterlony double diffusion. Due to lack of interspecies cross reactivity to mouse or rat ascites fluids, this antibody is also ideal for screening human monoclonal antibodies produced by hybridoma cells grown in vivo.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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The contribution of membrane interfacial interactions to recognition of membrane-embedded antigens by antibodies is currently unclear. This report demonstrates the optimization of this type of antibodies via chemical modification of regions near the membrane but not directly involved in the

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