Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. IgG is usually found as a monomer. IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. About 70 percent of the total immunoglobulin consists of IgG. Immunoglobulin M (IgM ) is a high molecular weight protein that has five or six subunits. It is the first immunoglobulin produced by neonates.
Anti-Human Polyvalent Immunoglobulins (G,A,M) antibody produced in rabbit has been used in enzyme-linked immunosorbent assay (ELISA) and sandwich ELISA.
Anti-Human Polyvalent Immunoglobulins (G,A,M) antibody produced in rabbit was used in sandwich ELISA as a standard.
Immunoglobulin M (IgM) acts as an antigen specific part of the B cell antigen receptor on the surface of B lymphocytes that are not stimulated, in its monomeric form. Polymeric IgM molecules also serve as important activators of the classical complement cascade. IgM is essential in agglutination and cytolytic reactions. Immunoglobulin G (IgG) participates in hypersensitivity type II and type III.
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 defence of the neonate against infections. IgA antibody is secretory antibody and is present abundantly in mucous linings of gastrointestinal, respiratory and genitourinary tracts, tears and saliva. IgM antibodies are present as pentamers in the serum and are produced in response to antigens.
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