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  2. Immunoglobulin G - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_G

    The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.

  3. Fragment crystallizable region - Wikipedia

    en.wikipedia.org/wiki/Fragment_crystallizable_region

    This region allows antibodies to activate the immune system, for example, through binding to Fc receptors. In IgG , IgA and IgD antibody isotypes , the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains ; IgM and IgE Fc regions contain three heavy chain ...

  4. Complement-dependent cytotoxicity - Wikipedia

    en.wikipedia.org/wiki/Complement-dependent_cyto...

    Complement-dependent cytotoxicity (CDC) is an effector function of IgG and IgM antibodies.When they are bound to surface antigen on target cell (e.g. bacterial or viral infected cell), the classical complement pathway is triggered by bonding protein C1q to these antibodies, resulting in formation of a membrane attack complex (MAC) and target cell lysis.

  5. Isotype (immunology) - Wikipedia

    en.wikipedia.org/wiki/Isotype_(immunology)

    The IgG, IgE and IgA antibody isotypes are generated following class-switching during germinal centre reaction and provide different effector functions in response to specific antigens. IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and ...

  6. Immunoglobulin superfamily - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_superfamily

    Molecule function/category Examples Description Antigen receptors: Antibodies or immunoglobulins: IgA IgD IgE IgG IgM; T-cell receptor chains; Antigen receptors found on the surface of T and B lymphocytes in all jawed vertebrates belong to the IgSF. Immunoglobulin molecules (the antigen receptors of B cells) are the founding members of the IgSF.

  7. Fc receptor - Wikipedia

    en.wikipedia.org/wiki/Fc_receptor

    For example, those that bind the most common class of antibody, IgG, are called Fc-gamma receptors (FcγR), those that bind IgA are called Fc-alpha receptors (FcαR) and those that bind IgE are called Fc-epsilon receptors (FcεR). The classes of FcRs are also distinguished by the cells that express them (macrophages, granulocytes, natural ...

  8. Anti-immunoglobulin - Wikipedia

    en.wikipedia.org/wiki/Anti-immunoglobulin

    Anti-Pan-Primate Antibody Type Description; Anti-Pan-Primate IgG [8F1] This is a recombinant monoclonal antibody to pan-primate IgG. This antibody reacts with most primate IgG antibodies, including human IgG. In a research setting the antibody has been used via ELISA to count IgG in supernatants from lung and lymph node tissues from cynomolgus ...

  9. Antibody - Wikipedia

    en.wikipedia.org/wiki/Antibody

    Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.