Anti-Monkey IgG (whole molecule)−Peroxidase antibody produced in rabbit

Immunoglobulins (Igs) have two heavy (H) and two light (L) chains, held together by disulphide linkages. They belong to the immunoglobulin super-family. The heavy chain has one variable N-terminal region and three to four constant (CH1-CH4) C-terminal regions. The light chain has one variable and constant region. IgGs are subclassified into IgG1, IgG2, IgG3 and IgG4.

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.

Rabbit polyclonal anti-Monkey IgG (whole molecule)−Peroxidase antibody recognizes monkey IgG in vitro and in monkey serum and biological fluids.

monkey IgG (rhesus)

Anti-Monkey IgG (whole molecule)−Peroxidase antibody produced in rabbit has been used in ELISA of serum samples.

Rabbit polyclonal anti-Monkey IgG (whole molecule)−Peroxidase antibody may be used to detect and quantitate the level of IgG in monkey serum and biological fluids via chromogenic, chemoluminescent or fluorogenic immunochemical or immunohistochemical techniques. It may also be used as a secondary antibody in assays that use monkey IgG as the primary antibody. It may be use to detect parasite-specific antibodies in monkey sera, ELISA assays were performed using HRP-conjugated rabbit anti-monkey IgG as the secondary.

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.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

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