ANTI-IMMUNOGLOBULIN G, HUMAN, FC, HRP

Peroxidase-conjugated goat anti-human IgG (Fc′ specific) antibody was used to detect the level of IgG activity in human plasma samples after treatment with rifin proteins by ELISA (1:50000).

Human IgGs are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. IgGs have four distinct isoforms, ranging from IgG1 to IgG4. The gene encoding IgG gene cluster is mapped to human chromosome 14. These antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders.
The antibody is isolated from anti-human IgG antiserum by immunospecific purification to remove essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fc fragment of human IgG. Anti-Human IgG is conjugated to peroxidase and is purified to remove unconjugated material.
Specificity and cross-reactivity of the Anti-Human IgG (Fc specific)-Peroxidase is determined by ELISA. The conjugate is specific for human IgG (Fc fragment) when tested against human IgA, IgG (Fab and Fc fragments), IgM, Bence Jones kappa, and lambda myeloma proteins. Furthermore, the conjugate shows no reactivity with mouse or rat IgG and yields reduced background with mouse or rat samples.

Antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders. Glycosylation is critical for IgG function. IgG subclasses have therapeutic potential against bacterial and viral infections. Gene translocation of the immunoglobulin heavy chain is associated in pathogenesis of multiple myeloma.