Anti-Mouse IgG IgA IgM (H+L) antibody produced in goat

Immunoglobulins (Igs) or antibodies are Y-shaped molecules which are the secreted form of the B-cell receptor. Igs are composed of two heavy and two light chains. An immunoglobulin possesses variable (V) domains that bind to antigens and constant (C) domains that bind to effector molecules. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as fragment antigen binding (Fab) fragments. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with 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. There are five classes of immunoglobulins- IgM, IgA, IgG, IgD and IgE, classified based on their C regions.

This product was prepared from polyspecific antiserum by immunoaffinity chromatography using antigens 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-Goat Serum, Mouse IgG, Mouse IgA and Mouse IgM.

Mouse IgG IgA and IgM whole molecule

Antibody format: IgG

Supplied in 0.1 M Sodium Borate, 0.075 M Sodium Chloride, 0.005 M EDTA, pH 8.0

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