Application

Anti-Human IgG (γ-chain specific) antibody was used as a standard in ELISA and radioimmunoassay.

Biochem/physiol Actions

IgG1 class is the most abundant and its deficiency results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions and IgG4 is associated with asymptomatic infection. Digestion of IgG by papain results in generation of fragment antigen binding (Fab). Pepsin digestion of IgG results in fragment crystallizable (Fc). The Fc region of IgG antibody has enormous therapeutic potential and is exploited for the development of therapeutic antibodies.

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General description

IgG antibody subtype is the most abundant 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 defence of the neonate against infections. Anti-Human IgG (γ-chain specific) antibody is specific for γ chain of all human IgG subclasses.

Immunoglobulins (Igs) belong to the immunoglobulin super-family and have two heavy (H) and two light (L) chains, held together by disulphide linkages. The L chain comprises of one variable N-terminal region and a constant C-terminal region. The heavy chain has one variable N-terminal region and three to four constant (CH1-CH4) C-terminal regions. IgG is an abundant protein in human serum. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4. The IgG heavy chain region is mapped to human chromosome 14.

Immunogen

Purified human IgG

Physical form

Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2