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

Antibody format: IgG

Immunoglobulin G (IgG), a member of the immunoglobulin family, 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. The primary structure of IgG 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.

Bovine IgG F(c) fragment

Anti-Bovine IgG (Fc specific) antibody produced in rabbit has been used in Western Blotting.

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. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Rabbit Serum, Bovine IgG, Bovine IgG F(c) and Bovine Serum. No reaction was observed against Bovine IgG F(ab′)2.

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

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