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Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains. These chains are held together by disulfide bonds. The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
In immunology, antibodies (immunoglobulins (Ig)) are classified into several types called isotypes or classes. The variable (V) regions near the tip of the antibody can differ from molecule to molecule in countless ways, allowing it to specifically target an antigen (or more exactly, an epitope). In contrast, the constant (C) regions only occur ...
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 .
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.
An antibody digested by papain yields three fragments, two Fab fragments and one Fc fragment An antibody digested by pepsin yields two fragments: a F(ab') 2 fragment and a pFc' fragment The fragment crystallizable region ( Fc region ) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some ...
Isoantibodies, formerly called alloantibodies, are antibodies produced by an individual against isoantigens produced by members of the same species. In the case of the species Homo sapiens, for example, there are a significant number of antigens that are different in every individual. When antigens from another individual are introduced 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.
Secondary antibodies provide signal detection and amplification along with extending the utility of an antibody through conjugation to proteins. [1] Secondary antibodies are especially efficient in immunolabeling. Secondary antibodies bind to primary antibodies, which are directly bound to the target antigen(s).