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  2. Antibody - Wikipedia

    en.wikipedia.org/wiki/Antibody

    Isotype or class switching is a biological process occurring after activation of the B cell, which allows the cell to produce different classes of antibody (IgA, IgE, or IgG). [64] The different classes of antibody, and thus effector functions, are defined by the constant (C) regions of the immunoglobulin heavy chain.

  3. 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 ...

  4. Immunoglobulin D - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_D

    Some antibodies form polymers that bind to multiple antigen molecules.. Immunoglobulin D (IgD) is an antibody isotype that makes up about 1% of proteins in the plasma membranes of immature B-lymphocytes where it is usually co-expressed with another cell surface antibody called IgM.

  5. Immunoglobulin class switching - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_class_switching

    Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]

  6. 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.

  7. 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.

  8. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    The immunoglobulin heavy chain (IgH) is the large polypeptide subunit of an antibody (immunoglobulin). In human genome, the IgH gene loci are on chromosome 14. A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains. Several different types of heavy chain exist that define the class or isotype of an ...

  9. Immune system - Wikipedia

    en.wikipedia.org/wiki/Immune_system

    Sometimes antibodies are generated against tumor cells allowing for their destruction by the complement system. [139] Some tumors evade the immune system and go on to become cancers. [145] [146] Tumor cells often have a reduced number of MHC class I molecules on their surface, thus avoiding detection by killer T cells.