Human IgG4-Fc Recombinant Protein (RPES2134)

Human IgG4-Fc Recombinant Protein

Immunoglobulin G (IgG) is the only monomeric immunoglobulin that can pass through the human placenta and is synthesized and released by plasma B cells. It constitutes 75% of serum immunoglobulins in humans, and it is a monomeric immunoglobulin involved in the secondary antibody response. IgG antibodies neutralize pathogens by agglutination and immobilization, complement activation, toxin neutralization, and antibody-dependent cell-mediated cytotoxicity. The IgG tetramer consists of two heavy chains (50 kDa) and two light chains (25 kDa), linked by disulfide bonds, with the two identical halves forming the Y-like form. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). The first immunoglobulin class in humans, IgG1 is most prevalent in blood and binds to Fc receptors (FcR ) on phagocytic cells with great affinity. For example, the Fc fragment of IgG is shown to mediate phagocytosis; cause inflammation, and selectively target Ig in specific tissues. Protein G or Protein A, which is on the surface of certain Staphylococcal and Streptococcal bacteria, specifically binds with the Fc region of IgGs; and it has several uses in biotechnology as a reagent for affinity purification. The recombinant immunoglobulin G Fc region is considered to be a potential anti-inflammatory therapy for human autoimmune diseases. Human IgG4-Fc Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.