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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. Antibody - Wikipedia

    en.wikipedia.org/wiki/Antibody

    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. Antibodies can recognize virtually any size antigen with diverse chemical compositions from ...

  4. 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 ...

  5. Coombs test - Wikipedia

    en.wikipedia.org/wiki/Coombs_test

    IgG antibodies are most reactive at 37°C. IgM antibodies are easily detected in saline at room temperature as IgM antibodies are able to bridge between RBC's owing to their large size, efficiently creating what is seen as agglutination. IgG antibodies are smaller and require assistance to bridge well enough to form a visual agglutination ...

  6. 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 ...

  7. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    An antibody molecule. The two heavy chains are colored red, blue, and purple. The two light chains green and yellow. See also: The immunoglobulin light chain is the small polypeptide subunit of an antibody (immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.

  8. Immunoglobulin therapy - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_therapy

    Immunoglobulin therapy is the use of a mixture of antibodies (normal human immunoglobulin) to treat several health conditions. [13] [14] These conditions include primary immunodeficiency, immune thrombocytopenic purpura, chronic inflammatory demyelinating polyneuropathy, Kawasaki disease, certain cases of HIV/AIDS and measles, Guillain–Barré syndrome, and certain other infections when a ...

  9. Passive immunity - Wikipedia

    en.wikipedia.org/wiki/Passive_immunity

    Immunoglobulin G (IgG) is the only antibody isotype that can pass through the human placenta, and is the most common antibody of the five types of antibodies found in the body. IgG antibodies protects against bacterial and viral infections in fetuses. Immunization is often required shortly following birth to prevent diseases in newborns such as ...

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