Anti-Mouse IgG (H+L)-Rhodamine 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. Pepsin cleaves the carboxy-terminal side of the disulfide bonds in the general region of the antibody and this gives rise to the F(ab′)2 fragment. The two antigen-binding arms of the antibody are linked in this fragment. 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 Mouse 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-Donkey Serum, Mouse IgG and Mouse Serum.

Mouse 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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