Anti-Goat IgG F(ab′)₂-Peroxidase antibody produced in rabbit

Immunoglobulin G (IgG) is part of the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150 kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50 kDa and 25 kDa respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, 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.

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Goat IgG coupled to agarose beads. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Rabbit Serum, Goat IgG, Goat IgG F(ab′)2 and Goat Serum. No reaction was observed against Goat IgG F(c).

Goat IgG F(ab′)2 fragment

Antibody format: IgG

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 1.0 mL deionized water (or equivalent).

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