Anti-Goat IgG (whole molecule)−R-Phycoerythrin antibody produced in rabbit

Immunoglobulins (Igs) belongs to the immunoglobulin super-family. Each immunoglobin has two heavy (H) and two light (L) chains, held together by disulphide linkages. Heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal region. Each light chain comprises of one variable N-terminal region and a constant C-terminal region. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4, among them IgG1 is most abundant.

Primary goat antibodies are often used to study target proteins for various clinical and research purposes. Thus, secondary antibodies against goat IgGs can be used to facilitate the accurate detection and localization of target proteins. Specificity of anti-goat IgG (whole molecule) has been tested by immunoelectrophoresis versus goat serum and goat IgG, prior to conjugation with R-Phycoerythrin.

Purified goat IgG

Anti-Goat IgG (whole molecule)-R-Phycoerythrin antibody is suitable for use in indirect immunofluorescence (1:20).

Anti-Goat IgG (whole molecule)−R-Phycoerythrin antibody produced in rabbit has been used in immunoassay.

Pepsin digestion of IgG results in fragment crystallisable (fc), with a H chain constant region. Papain digestion of IgG generates fragment antigen binding (Fab) with one complete light(L) chain and a variable and CH1 region of heavy(H) chain. IgG antibody have enormous therapeutic potential. Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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