Immunoglobulin G (IgG) is made up of four polypeptide chains: two heavy chains (γ chains) and two light chains (κ or λ chains) which are inter linked by disulfide bonds. The Fab (fragment antigen binding) arm of IgG is formed by the VH and CH1 domains of the heavy and the light chains. The V regions of the antibody serve as the antigen-binding region. IgG class of immunoglobulins consists of four sub-classes i.e IgG1, IgG2, IgG3, and IgG4.. T
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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.
Immunoglobulin G (IgG) is a group of antibodies that are involved in modulating various immune responses. IgG activates the complement system and regulates the antibody-dependent cell-mediated cytotoxicity (ADCC).
Physical form
Rabbit Anti-Rat IgG is supplied as a liquid containing 0.1% sodium azide (see MSDS) as preservative.
Preparation Note
treated to remove lipoproteins
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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
Pediatrics international : official journal of the Japan Pediatric Society, 42(4), 337-342 (2000-09-15)
Maternal immunoglobulin G (IgG), transferred across the placenta to the fetus during intrauterine life, is an important component of the neonatal immunological defence mechanisms against infection. There is controversy with respect to differences in placental transfer of the different IgG
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