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Anti-Saccharomyces cerevisiae antibodies (ASCAs) are antibodies against antigens presented by the cell wall of the yeast Saccharomyces cerevisiae. These antibodies are directed against oligomannose sequences α-1,3 Man (α-1,2 Man α-1,2 Man) n (n = 1 or 2). [ 1 ]
The direct Coombs test detects antibodies that are stuck to the surface of the red blood cells. [1] Since these antibodies sometimes destroy red blood cells they can cause anemia; this test can help clarify the condition. The indirect Coombs test detects antibodies that are floating freely in the blood. [1]
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 ...
This is a recombinant monoclonal antibody to IgG. When using ELISA, the anti-antibody also recognizes rhesus macaque IgG1, cynomolgus monkey IgG1, and cynomolgus monkey IgG4. [10] Anti-IgG3 [NH3/15.8] This is a recombinant monoclonal antibody to IgG3. Anti-IgG3 [NH3/15.8] is most commonly used in human IgG blood transfusion serology testing. [11]
An earlier publication suggested that the human ubiquitin-protein ligase E3 component n-recognin 2 (UBR2) was an important antigen [6] but follow up studies suggested this finding is likely to be an artifact. [7] Hence improved diagnosis, understanding and treatment of autoimmune pancreatitis awaits the identification of the auto-antigens involved.
The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
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]
This region allows antibodies to activate the immune system, for example, through binding to Fc receptors. In IgG , IgA and IgD antibody isotypes , the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains ; IgM and IgE Fc regions contain three heavy chain ...