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  2. Hypergammaglobulinemia - Wikipedia

    en.wikipedia.org/wiki/Hypergammaglobulinemia

    Hypergammaglobulinemia is a condition that is characterized by the increased levels of a certain immunoglobulin in the blood serum. [1] The name of the disorder refers to an excess of proteins after serum protein electrophoresis (found in the gammaglobulin region).

  3. IgA specific serine endopeptidase - Wikipedia

    en.wikipedia.org/wiki/IgA_specific_serine_endo...

    IgA protease (EC 3.4.21.72, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A protease, immunoglobulin A proteinase) is an enzyme. [ 1 ] [ 2 ] This enzyme catalyses the following chemical reaction [reaction equation needed]

  4. Immunoglobulin A - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_A

    The high prevalence of IgA in mucosal areas is a result of a cooperation between plasma cells that produce polymeric IgA (pIgA), and mucosal epithelial cells that express polymeric immunoglobulin receptor (pIgR). [15] Polymeric IgA (mainly the secretory dimer) is produced by plasma cells in the lamina propria adjacent to

  5. Serum protein electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Serum_protein_electrophoresis

    IgA has the most anodal mobility and typically migrates in the region between the beta and gamma zones also causing a beta/gamma fusion in patients with cirrhosis, respiratory infection, skin disease, or rheumatoid arthritis (increased IgA). Fibrinogen from plasma samples will be seen in the beta gamma region. Fibrinogen, a beta-2 protein, is ...

  6. Isotype (immunology) - Wikipedia

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

    The IgG, IgE and IgA antibody isotypes are generated following class-switching during germinal centre reaction and provide different effector functions in response to specific antigens. IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and ...

  7. 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.

  8. 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]

  9. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.

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