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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.
This is a recombinant monoclonal antibody to human IgG. It has the ability to bind to all 4 human IgG subtypes: IgG1, IgG2, IgG3, and IgG4. [7] Anti-Human IgG [8E11] This is a recombinant monoclonal antibody to human IgG. However, it can screen for IgG in nonhuman primates including vervets, chimpanzees, and mangabeys.
An antibody elution removes bound antibody from the surface of a red blood cell to aid in the antibody identification process. An antibody elution is a clinical laboratory diagnostic procedure which removes sensitized antibodies from red blood cells, in order to determine the blood group system antigen the antibody targets. [1]
IgG deficiency is a form of dysgammaglobulinemia where the proportional levels of the IgG isotype are reduced relative to other immunoglobulin isotypes.. IgG deficiency is often found in children as transient hypogammaglobulinemia of infancy, which may occur with or without additional decreases in IgA or IgM.
The direct Coombs test is used to detect antibodies or complement proteins attached to the surface of red blood cells. To perform the test, a blood sample is taken and the red blood cells are washed (removing the patient's plasma and unbound antibodies from the red blood cells) and then incubated with anti-human globulin ("Coombs reagent").
In chickens, immunoglobulin Y is the functional equivalent to Immunoglobulin G (IgG). Like IgG, it is composed of two light and two heavy chains. Structurally, these two types of immunoglobulin differ primarily in the heavy chains, which in IgY have a molecular mass of about 65,100 atomic mass units (amu), and are thus larger than in IgG.
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