IgG from rat serum

IgG (immunoglobulin G) antibody is enriched in mother′s milk. IgG is a major class of immunoglobulin. It 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.

IgG from rat serum has been used:

• To block programmed death ligand 1.
• As a control antibody to study the role of integrin b1 in spindle morphology
• In FACS (flow cytometry) staining
• ELISA (enzyme linked immunosorbent assay)

IgG from rat serum was used to block non-specific staining during FACS of peritoneal cells isolated from BALB/c mice. It was used as positive control in VDR staining of male and female breast tumor cells. IgG from rat serum was injected in control mice in tumor transplantation studies.

IgG antibody has its function similar to IgM antibody in complement system activation. IgG participates in hypersensitivity type II and type III. It helps in opsonization, complement fixation and antibody-dependent cell-mediated cytotoxicity.

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 7.2, containing 15 mM sodium azide

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