Immunoglobulins (Igs) belong to the immunoglobulin super-family. Each immunoglobin has two heavy (H) and two light (L) chains, held together by disulphide linkages. Heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal region. Each light chain comprises of one variable N-terminal region and a constant C-terminal region. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4, among them IgG1 is most abundant.

Anti-Bovine IgG (whole molecule) antibody produced in rabbit may be used for indirect ELISA at a working dilution of 1:150,000. It was used in fluorescence immunoassay for quantitative determination of IgG in bovine milk.

Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection. IgG antibody have enormous therapeutic potential and the Fc region is involved in the development of therapeutic antibody.

Digestion of IgG by papain results in generation of fragment antigen binding (Fab). Pepsin digestion of IgG results in fragment crystallisable (fc), comprises the H chain constant region. Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection. IgG antibody have enormous therapeutic potential and the Fc region is involved in the development of therapeutic antibody.

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.

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

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