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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.
[2] [3] CD32 has a low-affinity for the Fc region of IgG antibodies in monomeric form, but high affinity for IgG immune complexes. [4] CD32 has two major functions: cellular response regulation, and the uptake of immune complexes. [2] Cellular responses regulated by CD32 include phagocytosis, cytokine stimulation, and endocytic transport. [3]
Polyclonal antibodies (pAbs) are antibodies that are secreted by different B cell lineages within the body (whereas monoclonal antibodies come from a single cell lineage). They are a collection of immunoglobulin molecules that react against a specific antigen , each identifying a different epitope .
This list of over 500 monoclonal antibodies includes approved and investigational drugs as well as drugs that have been withdrawn from market; consequently, the column Use does not necessarily indicate clinical usage. See the list of FDA-approved therapeutic monoclonal antibodies in the monoclonal antibody therapy page.
An antibody is made up of two heavy chains and two light chains. The unique variable region allows an antibody to recognize its matching antigen. [73] A B cell identifies pathogens when antibodies on its surface bind to a specific foreign antigen. [74] This antigen/antibody complex is taken up by the B cell and processed by proteolysis into ...
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.
The same antibodies can be anchored to the surface of cells of the immune system, in which case they serve as receptors, or they can be secreted in the blood, known as soluble antibodies. On a molecular scale, the proteins are relatively large, so they cannot be recognized as a whole; instead, their segments, called epitopes, can be recognized. [1]
Antibodies of different classes activate distinct effector mechanisms in response to an antigen (triggering different elements of the innate immune system). They appear at different stages of an immune response, differ in structural features, and in their location around the body. [1] Isotype expression reflects the maturation stage of a B cell ...