Monkey IgG is a plasma B cell derived antibody isotype defined by its heavy chain. IgG is the most abundant antibody isotype found in monkey serum. IgG crosses the placental barrier, is a complement activator and binds to the Fc-receptors on phagocytic cells. The level of IgG may vary with the status of disease or infection.
Horseradish Peroxidase (HRP) is an enzyme that catalyzes the conversion of chromogenic substrates such as o-phenylenediamine (OPD), 4-chloro-1-naphthol 3,3′,5,5′-tetramethylbenzidine (TMB), 3,3′-Diaminobenzidine (DAB) or 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS); chemiluminescent substrates such as CPS-3 (enhanced luminal) and fluorogenic substrates such as Ampliflu Red into detectable chromophores, light-emitters or fluorescers, respectively.
Digestion of IgG by papain results in generation of fragment antigen binding (Fab). Pepsin digestion of IgG results in fragment crystallizable (Fc). Fc regions of IgG antibody have enormous therapeutic potential and are exploited for the development of therapeutic antibodies. IgG1 class is the most abundant and its deficiency results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions and IgG4 is associated with asymptomatic infection. The IgG levels in monkey show age related increase. In monkeys, IgG subtypes comprises the predominant antibodies during immune response after hepatitis B surface antigen (HBsAg) vaccination. The human and monkey IgG sequences show divergence only in the hinge region and hence exploited for therapeutic antibody testing.
