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Griffin:Antibody Basics: Difference between revisions
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[[Image:antibody1.jpg|thumb|right|The basic structure of the heterotetrameric, disfulfide linked, Immunoglobulin gamma (IgG)]] | [[Image:antibody1.jpg|thumb|right|The basic structure of the heterotetrameric, disfulfide linked, Immunoglobulin gamma (IgG)]] | ||
[http://en.wikipedia.org/wiki/Antibody Antibodies] are B cell (lymphocyte) derived proteins produced by the immune system in order to address the immunological needs of a mammalian system over time. The most common type of research antibody is the IgG that | [http://en.wikipedia.org/wiki/Antibody Antibodies] are B cell (lymphocyte) derived proteins produced by the immune system in order to address the immunological needs of a mammalian system over time. The most common type of research antibody is the IgG that contains 2 heavy chains (~50 kDa each) and 2 light chains (~25 kDa each). 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 to exist. This region is known as the hypervariable region (Fab). 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. | ||
===Fc fragment=== | ===Fc fragment=== | ||
