Immunoglobulins (Igs) belongs to immunoglobulin super-family (IgSF). Igs in general, consist of two heavy (H) chains and two light (L) chains. The L chain can be either κ or a λ chain. Each chain contains one NH2-terminal “variable" (V) region and one or more COOH-terminal “constant” (C) regions. Each of which consists of two sandwiched β pleated sheets ′pinned′ together by a disulfide bridge. There are five main classes of Igs based on heavy chain C domains, they are, IgM, IgG, IgA, IgD, and IgE isotypes. IgG can be divided into four subclasses, IgG1, IgG2, IgG3, and IgG4. Each subclass possesses distinct biologic properties.
Application
Anti-Human IgG (Fab specific), F(ab′)2 fragment antibody produced in goat has been used in enzyme linked immunosorbent assay (ELISA) and biosensor methodology.
Biochem/physiol Actions
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 digested by papain and yields two Fab fragments, each of which can bind antigen, and a single Fc fragment. IgG is split by pepsin splits into an Fc fragment and a single dimeric F(ab)2 that can cross-link as well as bind antigens.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% sodium azide as preservative
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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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