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What is an antibodie?

Updated: 12/21/2022
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14y ago

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Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.

Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.

The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.

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8y ago

An antibody is a protein produced by B-lymphocytes which binds to a specific antigen.

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Q: What is an antibodie?
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What is the super shift?

http://en.wikipedia.org/wiki/Electrophoretic_mobility_shift_assay A super shift is this technic. But we had an antibodie that recognizes the protein to create an even larger complex with a greater shift. The protein will move throught the gel with a vitess decrease or we won't detect the protein if the antibodie recognise the binding site of the protein.


Why do each pathogen need a specific antibody?

each pathogen has a antigene which the antibodies attach to so each pathogen needs a unique antibodie


Is an antibodie an antigen?

An antibody is a glycoprotein that is produced by plasma cells. It consists of heavy chains and light chains. An antigen is a molecule that interacts with an antibody (or T-Cell). When the antigen interaction induces an immune response it is known as an immunogen.