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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. 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.

  4. Paratope - Wikipedia

    en.wikipedia.org/wiki/Paratope

    Antibody crystallizable region (Fc) 3. Heavy chains 4. Light chains 5. Variable region of the antibody. The paratope is the key-shaped section that makes direct contact with the antigen. [1] 6. Hinge regions . In immunology, a paratope, also known as an antigen-binding site, is the part of an antibody which recognizes and binds to an antigen.

  5. File:Antibody basic unit.svg - Wikipedia

    en.wikipedia.org/wiki/File:Antibody_basic_unit.svg

    One of the two antigen-binding regions is circled: they are formed by the variable regions at the tip of the antibody. The heavy chains have (starting from the N-terminus at the tip) a variable domain (V H ), followed by a constant domain (C H 1), a hinge region, and two more constant domain (C H 2, C H 3).

  6. Complementarity-determining region - Wikipedia

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

    A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total. There are three CDR loops per variable domain in antibodies. 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.

  7. Immune system - Wikipedia

    en.wikipedia.org/wiki/Immune_system

    An antibody is made up of two heavy chains and two light chains. The unique variable region allows an antibody to recognize its matching antigen. [73] A B cell identifies pathogens when antibodies on its surface bind to a specific foreign antigen. [74] This antigen/antibody complex is taken up by the B cell and processed by proteolysis into ...

  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. Framework region - Wikipedia

    en.wikipedia.org/wiki/Framework_region

    Antibody humanization is an example of beneficial genetic engineering in medicine today. [10] Humanized antibody refers to the creation of non-human antibody in vivo and in response to antigen, then the isolation and humanization of the framework and constant regions. It has been discovered that while these antibodies remain relatively intact ...