Anti-Rat IgG (whole molecule)−Peroxidase antibody produced in goat

Anti-Rat IgG (whole molecule)-Peroxidase antibody is suitable for use in ELISA and immunoblot at 1:5000 dilutions.

Lysates generated from primary cells isolated from lymphoid organs of P. monodon shrimp were analyzed by western blot using HRP-conjugated goat anti-rat as the secondary antibody at a 1:4000 dilution.

IgG (immunoglobulin γ), upon epitope binding, mediates the activation of classical complement pathway. Interaction between the host cell membrane and IgG antibody results in type II hypersensitivity reaction. Decreased serum levels of IgG contributes to common variable immunodeficiency, thus making the individual easily prone to infections.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

IgGs are glycoprotein antibodies that modulate several immune responses. Rat IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rat IgG conjugated to a detectable substrate is a useful tool for the analysis of target proteins. Anti-Rat IgG (whole molecule)-Peroxidase antibody binds all rat immunoglobulins.
IgG (immunoglobulin γ) is a monomeric antibody containing a γ Fc region as a part of heavy chain, which is linked to the Fab arm through a hinge region. It is the most abundant serum antibody and constitutes to 70% of the total immunoglobulins.

Purified rat IgG

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin with preservative

Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).