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  2. 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 ]

  3. IGHE - Wikipedia

    en.wikipedia.org/wiki/IGHE

    IGHE (immunoglobulin heavy constant epsilon): The gene that encodes the ε heavy chain constant region for the IgE antibody. This gene is critical for the production and function of IgE in the body. The IGHE gene provides instructions for making a part of an antibody (immunoglobulin) called Immunoglobulin E, or IgE. [5]

  4. FCER1 - Wikipedia

    en.wikipedia.org/wiki/FCER1

    The high-affinity IgE receptor, also known as FcεRI, or Fc epsilon RI, is the high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotype involved in allergy disorders and parasite immunity. FcεRI is a tetrameric receptor complex that binds Fc portion of the ε heavy chain of IgE. [1]

  5. 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.

  6. 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.

  7. 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.

  8. These 89 Appetizers Might Just Be The Best Part Of ... - AOL

    www.aol.com/lifestyle/89-appetizers-might-just...

    Turkey Cheese Ball. Even if you're not serving turkey this Thanksgiving doesn't mean you can't get in on the theme. Enter: this adorable cheeseball.We used carrots, pecans, pretzels, and bell ...

  9. Immunoglobulin light chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_light_chain

    Free immunoglobulin light chains secreted by neoplastic plasma cells, such as in multiple myeloma, can be called Bence Jones protein when detected in the urine, although there is a trend to refer to these as urinary free light chains. Increased levels of free Ig light chains have also been detected in various inflammatory diseases.

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