Anti-Rabbit IgG (Fc specific) antibody produced in goat

Anti-Rabbit IgG (Fc specific) antibody produced in goat has been used in immunohistochemistry.

Anti-Rabbit IgG (Fc specific) antibody produced in goat has been used in immunohistochemistry.

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

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Antibody format: IgG

Immunoglobulin G (IgG) is a member of the immunoglobulin family and is a widely expressed serum antibody. 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 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 CH2 and CH3 domains of the antibody molecule. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

Immunoglobulin G (IgG) is made up 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 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 CH2 and CH3 domains of the antibody molecule. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

Rabbit IgG F(c) fragment

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