Immunoglobulin G (IgG) is a member of the immunoglobulin family and consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The Fc fragment contains the CH2 and CH3 domains of the antibody molecule. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.
Specificity
This product was prepared from monospecific antiserum by immunoaffinity chromatography using Sheep IgG coupled to agarose beads. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Rabbit Serum, Sheep IgG, Sheep IgG F(c) and Sheep Serum. No reaction was observed against Sheep IgG F(ab′)2.
Immunogen
Sheep IgG F(c) fragment
Physical properties
Antibody format: IgG
Physical form
Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
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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Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE and Story CM
Journal of Reproductive Immunology, 37(1), 1-23 (1997)
Antibody structure, instability, and formulation.
Wang W
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