Description
Immunoglobulins are membrane-bound or secreted glycoproteins produced by B lymphocytes. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as the antibody-dependent cell-mediated cytotoxicity. IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors on phagocytic cells with high affinity. IgG comprise two identical light (L) and heavy (H) chains forming a 'Y?shaped' structure. It also is digested by pepsin proteolysis into two distinct fragments (Fab, Fc). Fc fragment is a homodimeric glycoprotein with one monomer consisting of two constant immunoglobulin domains (CH2, CH3) from the C?terminal half of one heavy chain. Through interaction with its ligands (FcgammaR, C1q and FcRn) it mediates various immune effector functions and increases the half?life of the antibody molecule. Recombinant IgG Fc is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases. Recombinant human IgG1 Fc was expressed in HEK293 cell and purified by using conventional chromatography techniques