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  2. File:Immunoglobulin basic unit.svg - Wikipedia

    en.wikipedia.org/wiki/File:Immunoglobulin_basic...

    English: Schematic diagram of the basic unit of immunoglobulin (antibody) Fab; Fc; heavy chain (consist of VH, CH1, hinge, CH2 and CH3 regions: from N-term) light chain (consist of VL and CL regions: from N-term) antigen binding site; hinge regions (*) -S-S-mean disulfide bonds.

  3. 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.

  4. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    The two heavy chains are colored red and blue and the two light chains green and yellow. [1] 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.

  5. Complementarity-determining region - Wikipedia

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

    Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively. CDRs are where these molecules bind to their specific antigen and their structure/sequence determines the binding activity of the respective antibody.

  6. Framework region - Wikipedia

    en.wikipedia.org/wiki/Framework_region

    [5] [6] [7] Individual residues in the framework region can be divided into two categories, depending on whether they are in direct contact with the antigen. Framework residues that come in contact with the antigen are a part of the antibody's binding site, and are located either close in sequence to the CDRs or in close proximity to the CDR ...

  7. Immunoglobulin C2-set domain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_C2-set_domain

    There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4).

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  9. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    Once set, light chain class remains fixed for the life of the B lymphocyte. In a healthy individual, the total kappa-to-lambda ratio is roughly 2:1 in serum (measuring intact whole antibodies) or 1:1.5 if measuring free light chains, with a highly divergent ratio indicative of neoplasm. The free light chain ratio ranges from 0.26 to 1.65. [1]