Other Proteins

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(c) region, recognized by high-affinity Fc receptor proteins.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present.

Human IgG purified protein (Immunoglobulin G) are antibody molecules. Human IgG is composed of four peptide chains — two heavy chains gamma and two light chains. Human IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. Human IgG typically constitutes 75% of serum immunoglobulins. Human IgG molecules are synthesized and secreted by plasma B cells.

Human IgG F(ab')2 purified protein is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. Human IgG F(ab')2 molecules lack the Fc portion of Human IgG and therefore receptors that bind Human IgG Fc will not bind Human IgG F(ab')2 molecules.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsinization for phagocytosis. The F(ab) fragment is the portion of the antibody that binds to the antigen target. The immunoglobulin Fab also possesses one constant and one variable region of both the heavy and light chain.

Immunoglobulin A is the primary responder in muscosal immunity, and comprises close to 75% of the total immunoglobulin produced. IgA can also be secreted and is protected from degradation by many proteolytic enzymes (which allows it to be secreted along the gastrointestinal tract). Immunoglobulin A only weakly activates the complement system and is not readily opsonized.

Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. Formed from covalently linking 5 immunoglobulins together, the approximate molecular weight of IgM is 900kDa and possesses 10 binding sites (though due to the size of most antigens, not all sites are capable of binding at once). Due to this large size, IgM is typically isolated to the serum.