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  2. 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.

  3. Complementarity-determining region - Wikipedia

    en.wikipedia.org/wiki/Complementarity...

    Sixty CDRs can be found on a pentameric IgM molecule, which is composed of five antibodies and has increased avidity as a result of the collective affinity of all antigen-binding sites combined. Since most sequence variation associated with immunoglobulins and T cell receptors are found in the CDRs, these regions are sometimes referred to as ...

  4. Anti-immunoglobulin - Wikipedia

    en.wikipedia.org/wiki/Anti-immunoglobulin

    Specifically, anti-immunoglobulin antibodies are created by B-cells as antibodies to bind to other immunoglobulins. Immunoglobulins have two regions: the constant region and the variable region. The constant region is involved in effector function, while the variable region is involved in recognizing and binding to antigens .

  5. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    Other types of light chains can be found in lower vertebrates, such as the Ig-Light-Iota chain of Chondrichthyes and Teleostei. [3] [4] Camelids are unique among mammals as they also have fully functional antibodies which have two heavy chains, but lack the light chains usually paired with each heavy chain. [5]

  6. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    Heavy chains μ and ε have a constant region composed of four domains. [4] a variable region that differs between different B cells, but is the same for all immunoglobulins produced by the same B cell or B cell clone. The variable domain of any heavy chain is composed of a single immunoglobulin domain. These domains are about 110 amino acids ...

  7. Immunoglobulin M - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_M

    Immunoglobulin M (IgM) is the largest of several isotypes of antibodies (also known as immunoglobulin) that are produced by vertebrates.IgM is the first antibody to appear in the response to initial exposure to an antigen; [1] [2] causing it to also be called an acute phase antibody.

  8. Complement system - Wikipedia

    en.wikipedia.org/wiki/Complement_system

    Scheme of the complement system. The complement system, also known as complement cascade, is a part of the humoral, innate immune system and enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. [1]

  9. Organization and expression of immunoglobulin genes

    en.wikipedia.org/wiki/Organization_and...

    Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.