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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.
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.
Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]
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.
D-to-J recombination occurs first in the β-chain of the TCR. This process can involve either the joining of the D β 1 gene segment to one of six J β 1 segments or the joining of the D β 2 gene segment to one of six J β 2 segments. [3] DJ recombination is followed (as above) with V β-to-D β J β rearrangements.
Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.
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.