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  2. Immunoglobulin M - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_M

    Immunoglobulin M (IgM) is the largest of several isotypes of antibodies (also known as immunoglobulin) that are produced by vertebrates. IgM is the first antibody to appear in the response to initial exposure to an antigen ; [ 1 ] [ 2 ] causing it to also be called an acute phase antibody.

  3. Isotype (immunology) - Wikipedia

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

    Thus an antibody isotype is determined by the constant regions of the heavy chains only. [1] IgM is first expressed as a monomer on the surface of immature B cells. Upon antigenic stimulation, IgM+ B cells secrete pentameric IgM antibody formed by five Ig monomers which are linked via disulfide bonds.

  4. Anti-immunoglobulin - Wikipedia

    en.wikipedia.org/wiki/Anti-immunoglobulin

    This is a recombinant monoclonal antibody to IgM. The anti-antibody functions in early detection of antigens in serum rather than interstitial fluids. [13] Anti-IgM [B481] This is a recombinant monoclonal antibody to IgM. It is recommended to use anti-IgM [B481] as a secondary antibody against IgM primary antibodies. [14]

  5. 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.

  6. Coombs test - Wikipedia

    en.wikipedia.org/wiki/Coombs_test

    IgG antibodies are most reactive at 37°C. IgM antibodies are easily detected in saline at room temperature as IgM antibodies are able to bridge between RBC's owing to their large size, efficiently creating what is seen as agglutination. IgG antibodies are smaller and require assistance to bridge well enough to form a visual agglutination ...

  7. Immunoglobulin class switching - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_class_switching

    Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]

  8. ABO blood group system - Wikipedia

    en.wikipedia.org/wiki/ABO_blood_group_system

    The associated anti-A and anti-B antibodies are usually IgM antibodies, produced in the first years of life by sensitization to environmental substances such as food, bacteria, and viruses. The ABO blood types were discovered by Karl Landsteiner in 1901; he received the Nobel Prize in Physiology or Medicine in 1930 for this discovery. [ 5 ]

  9. J chain - Wikipedia

    en.wikipedia.org/wiki/J_chain

    The Joining (J) chain is a protein component that links monomers of antibodies IgM and IgA to form polymeric antibodies capable of secretion. [5] The J chain is well conserved in the animal kingdom , but its specific functions are yet to be fully understood.