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  2. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    Schematic diagram of a typical antibody showing two Ig heavy chains (blue) linked by disulfide bonds to two Ig light chains (green). The constant (C) and variable (V) domains are shown. An antibody molecule. The two heavy chains are colored red, blue, and purple. The two light chains green and yellow. See also:

  3. Antibody - Wikipedia

    en.wikipedia.org/wiki/Antibody

    Each antibody contains two identical light chains: both κ or both λ. Proportions of κ and λ types vary by species and can be used to detect abnormal proliferation of B cell clones. Other types of light chains, such as the iota (ι) chain, are found in other vertebrates like sharks (Chondrichthyes) and bony fishes . [citation needed]

  4. 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.

  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. File:Antibody basic unit.svg - Wikipedia

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

    The light chains have a variable domain (V L) and a constant domain (C L). The C H 2 and C H 3 regions form the crystallizable fragment (Fc). The variable and C H 1, C L regions form a pair of antigen-binding fragments (Fab). Disulfide bonds between the chains are drawn as S-S. Their exact number and location varies for different isotypes.

  7. Immunoglobulin D - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_D

    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. IgD is also produced in a secreted form that is found in very small amounts in blood serum, representing 0.25% of immunoglobulins in serum.

  8. Framework region - Wikipedia

    en.wikipedia.org/wiki/Framework_region

    The universal structure of antibody includes the constant regions part of the fragment crystallizable(Fc) region of the antibody (shown in dark blue). It also includes the fragment antigen binding which is composed of one heavy and one light chain (shown as L for light and H for heavy).

  9. Immunoglobulin A - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_A

    Colors are: H-chains (blue and light blue), L-chains (red and light red), J-chain (magenta) and the secretory component (yellow). Coordinates of each backbone carbon atom were derived PDB entry 3cm9. [2] Immunoglobulin A (Ig A, also referred to as sIgA in its secretory form) is an antibody that plays a role in the immune function of mucous ...