HUMAN IgG whole molecule, Phycoerythrin conjugated

Human IgG whole molecule Phycoerythrin conjugated was prepared from normal serum delipidation, salt fractionation, ion exchange chromatography followed by extensive dialysis against the buffer stated above.  Human IgG whole molecule Phycoerythrin conjugated was assayed by immunoelectrophoresis resulted in a single precipitin arc against anti-Phycoerythrin, anti-Human IgG and anti-Human Serum. 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 whole IgG molecule possesses both the F(c) region, recognized by high-afinity 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. This Human IgG whole molecule is conjugated to biotin (Vitamin H), a small biomolecule that has a large affinity for avidin and streptavidin.