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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
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.
IgA: immunoglobulin A: IgAV: IgA vasculitis (formerly known as Henoch–Schönlein purpura) IgD: immunoglobulin D: IgE: immunoglobulin E: IGF: insulin-like growth factor IgG: immunoglobulin G: IgG4-RD: IgG4-related disease: IgG4-RKD: IgG4-related kidney disease IgG4-ROD: IgG4-related ophthalmic disease: IgG4-TIN: IgG4-related tubulointerstitial ...
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 ...
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 ...
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]
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]
The J chain's primary structure is unusually acidic having a high content of negatively charged amino acids. [11] It has 8 cysteine residues, 6 of which are involved in intramolecular disulfide bonds while the remaining two function to bind the Fc tailpiece regions of IgA or IgM antibodies, the α chain and μ chain respectively.
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