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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.
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.
These heavy chain types vary between different animals. All heavy chains contain a series of immunoglobulin domains, usually with one variable domain (V H) that is important for binding antigen and several constant domains (C H 1, C H 2, etc.). Production of a viable heavy chain is a key step in B cell maturation.
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain. [1] [2] The Fc regions of IgGs bear a highly ...
A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total. There are three CDR loops per variable domain in antibodies. Sixty CDRs can be found on a pentameric IgM molecule, which is composed of five antibodies and has increased avidity as a result of the collective affinity of all antigen-binding sites combined.
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β-sheets.
This is a recombinant monoclonal antibody to Pan-primate IgG. The antibody reacts to most primate IgG, including human IgG. The most important use of anti-Pan-primate is to quantify IgG in homogenates from macaque lungs and lymph nodes. [9] Anti-IgG [NH3/130.5.2] This is a recombinant monoclonal antibody to IgG.
It has the shortest half-life compared to the other IgG subclasses [11] and is frequently present together with IgG1 in response to protein antigens after viral infections. [12] IgG4 is the least abundant IgG subclass in the serum and is often generated following repeated exposure to the same antigen or during persistent infections.