IgG (immunoglobulin G) antibody is enriched in mother′s milk. IgG contributes to 10−20% of plasma protein and is regarded as one of the most abundant serum protein. It consists of four subclasses : IgG1, IgG2, IgG3 and IgG4. The IgG structure possesses four polypeptide chains containing two identical γ heavy (H) chains and two identical κ or λ light (L) chains of 50kDa and 25kDa respectively. The chains are interlinked with a disulfide bond. Both the L and the H chains consist of a variable domain at the N-terminal. The C-terminal bears′ constant domains: three in H chain with a hinge region and one in the L chain. The variable region of IgG antibody is specific to antigens and is highly conserved.
Binds all mouse IgGs (minimal cross-reaction with human, bovine, horse, rabbit and swine serum proteins)
IgG (immunoglobulin G) antibody protects against bacterial, fungal and viral infections. IgG antibody has its function similar to IgM antibody in complement system activation. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections. IgG participates in hypersensitivity type II and type III. It helps in opsonization, complement fixation and antibody dependent cell mediated cytotoxicity.
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Supplied in phosphate buffered saline with 0.05% sodium azide, 50% glycerol and 2 mg/mL bovine serum albumin.
Protect from light.
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