Anti-Human IgG (Fc specific) antibody produced in rabbit

Immunoglobulin G (IgG) belongs to the immunoglobulin family. It is widely expressed and consists of a gamma (γ) heavy chain in the constant (C) region. IgG is a monomer with a molecular weight of about 150 kDa. The 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. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The Fc fragment contains the C_H2 and C_H3 domains of the antibody molecule. 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 Human IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Rabbit Serum, Human IgG, Human IgG F(c) and Human Serum. No reaction was observed against Human IgG F(ab′)2.

Human IgG F(c) fragment

Anti-Human IgG (Fc specific) antibody produced in rabbit has been used as a control in cysteine-rich angiogenic inducer 61 (CYR61) blocking experiment.

Antibody format: IgG

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

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