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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.
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.
Immunoglobulin A (Ig A, also referred to as sIgA in its secretory form) is an antibody that plays a role in the immune function of mucous membranes. The amount of IgA produced in association with mucosal membranes is greater than all other types of antibody combined. [ 3 ]
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 ...
In addition, immunochemistry is the study of the identities and functions of the components of the immune system. Immunochemistry is also used to describe the application of immune system components, in particular antibodies, to chemically labelled antigen molecules for visualization.
Humoral immunity is also referred to as antibody-mediated immunity. The study of the molecular and cellular components that form the immune system , including their function and interaction, is the central science of immunology .
The resulting antibodies are designated IgW (also called IgX or IgNARC) and IgNAR (immunoglobulin new antigen receptor). [ 13 ] [ 14 ] The latter type is a heavy-chain antibody , an antibody lacking light chains, and can be used to produce single-domain antibodies , which are essentially the variable domain (V NAR ) of an IgNAR.
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.