Human IgG2-Fc Recombinant Protein (RPES2176)

Human IgG2-Fc Recombinant Protein

Immunoglobulins have a variety of functions in the body, including the following: IgG is synthesized and secreted by plasma B cells as a monomeric immunoglobulin that is primarily active in the secondary antibody response and only one kind that may pass through the human placenta. The presence of anti-IgG antibodies protects against infections by agglutination and immobilization, complement activation, toxin neutralization, and antibody-dependent cell-mediated cytotoxicity (ADCC).IgG tetramer consists of two heavy chains (50kDa) and two light chains (25kDa), linked by disulfide bonds, which forms a Y-shaped pattern. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). The most prevalent immunoglobulin G, IgG1 binds to Fc receptors (FcR ) with great affinity on phagocytic cells. Fc fragment is demonstrated to mediate phagocytosis; trigger inflammation, and target Ig to particular tissues. Protein G or Protein A 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 an affinity purification reagent. The recombinant IgG Fc region is thought to be a potential anti-inflammatory medication for the treatment of human immunological disorders. Human IgG2-Fc Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.