Anti-Bovine IgG (H+L), F(ab′)₂ fragment-Peroxidase antibody produced in rabbit

IgG (immunoglobulin G) contributes to 10−20% of plasma protein and is regarded as one of the most predominant serum protein. It consists of four subclasses: IgG1, IgG2, IgG3 and IgG4. The IgG structure possesses four polypeptide chains containing two identical γ heavy (H) chains and two identical κ or λ light (L) chains of 50kDa and 25kDa respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as fragment antigen binding (Fab) fragments. These fragments contain the light chains paired with the VH and CH1 domains of the heavy chains. The variable region of IgG antibody is specific to antigens and is highly conserved. IgG antibody is abundantly present in mother′s milk.

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Bovine IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities, pepsin digestion and chromatographic separation. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Rabbit Serum, Bovine IgG and Bovine Serum. No reaction was observed against Anti-Pepsin or Anti-Rabbit IgG F(c).

Bovine IgG whole molecule

IgG (immunoglobulin G) antibody provides protection against bacterial, fungal and viral infections. Maternal IgG is transferred to fetus through the placenta that is vital for the immune defense of the neonate against infections. IgG antibody has its function similar to IgM antibody in complement system activation. IgG is involved in hypersensitivity type II and type III. It helps in opsonization, complement fixation and cell-mediated cytotoxicity.

Antibody format: IgG F(ab′)2

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free

Reconstitute with 500 μ;L deionized water (or equivalent).

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