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F4012

Sigma-Aldrich

Anti-Dog IgG (whole molecule)–FITC antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Rabbit Anti-Dog IgG (whole molecule)–Fluorescein isothiocyanate

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About This Item

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

biological source

rabbit

Quality Level

conjugate

FITC conjugate

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

storage condition

protect from light

technique(s)

direct immunofluorescence: 1:32

storage temp.

−20°C

target post-translational modification

unmodified

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General description

IgG is present in large quantities in the human serum and 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 (γ chains) 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-Dog IgG (whole molecule)-FITC antibody has been used in indirect fluorescent antibody test(IFAT)
Rabbit polyclonal anti-Dog IgG (whole molecule)–FITC antibody may be used as a secondary antibody or to detect the presence of dog IgG via fluorogenic immunochemical or immunohistochemical techniques.

Biochem/physiol Actions

IgG, a monoclonal antibody can be cleaved at the hinge region by nonspecific proteases like papain and pepsin. This can result in univalent Fab fragments or bivalent F(ab′)2 fragments. These two enzymes have a broad substrate specificity resulting in heterogenous fragments. Fluorescein isothiocyanate (FITC) is a fluorescein derivative (fluorochrome) used to tag antibodies, including secondary antibodies, for use in fluorescence-based assays and procedures. FITC excites at 495nm and emits at 521nm.

Physical form

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

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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Experimental inoculation of Neospora caninum tachyzoites in eared doves (Zenaida auriculata)
de Barros L D, et al.
Experimental Parasitology, 202(1-2), 1-6 (2019)
Alexandre Dias Munhoz et al.
Veterinary parasitology, 206(3-4), 123-128 (2014-12-04)
The aim of this study was to experimentally evaluate infection in Gallus gallus domesticus with Neospora caninum tachyzoites of the NC-1 strain. Experimental infection was conducted in 90-day-old chickens, embryonated eggs and bioassays in dogs. In the first experiment, poults
Papain digestion of different mouse IgG subclasses as studied by electrospray mass spectrometry
Adamczyk M, et al.
Journal of Immunological Methods, 237(1-2), 95-104 (2000)
Jacqueline Fischer-Lougheed et al.
Immunology, 123(3), 390-397 (2007-10-06)
Synthetic anti-idiotypic antibodies represent a potentially valuable tool for the isolation and characterization of B cells that produce xenoantibodies. An anti-idiotypic antibody that binds to a subset of B cells producing antibodies encoded by the variable-region heavy chain 3 (V(H)3)
Gestur Vidarsson et al.
Frontiers in immunology, 5, 520-520 (2014-11-05)
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These

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