enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    Only one type of light chain is present in a typical antibody, thus the two light chains of an individual antibody are identical. Each light chain is composed of two tandem immunoglobulin domains: one constant (C L) domain; one variable domain (V L) that is important for binding antigen; The approximate length of a light chain protein is from ...

  3. Fragment antigen-binding region - Wikipedia

    en.wikipedia.org/wiki/Fragment_antigen-binding...

    Structure of a Fab with light and heavy chains. The fragment antigen-binding region (Fab region) is a region on an antibody that binds to antigens.It is composed of one constant and one variable domain of each of the heavy and the light chain.

  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. Allotype (immunology) - Wikipedia

    en.wikipedia.org/wiki/Allotype_(immunology)

    In immunology, allotype is an immunoglobulin variation (in addition to isotypic variation) that can be found among antibody classes and is manifested by heterogeneity of immunoglobulins present in a single vertebrate species. The structure of immunoglobulin polypeptide chain is dictated and controlled by number of genes encoded in the germ line ...

  6. 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.

  7. 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.

  8. 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 ...

  9. Immunoglobulin E - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_E

    Immunoglobulin E (IgE) is a type of antibody (or immunoglobulin (Ig) "isoform") that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains (ε chain) and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). [1]