Anti-Rabbit IgG (H+L)-Peroxidase antibody produced in donkey

Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa 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 (called Fab fragments) and contain the antigen-binding activity. The third fragment (called Fc fragment) does not possess antigen-binding activity, but binds to cells and effector molecules. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Rabbit IgG coupled to agarose beads. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Donkey Serum, Rabbit IgG and Rabbit Serum.

Rabbit IgG whole molecule

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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