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2. Immunoglobulin G - Wikipedia

   en.wikipedia.org/wiki/Immunoglobulin_G

   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.

3. Organization and expression of immunoglobulin genes

   en.wikipedia.org/wiki/Organization_and...

   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.

4. Anti-immunoglobulin - Wikipedia

   en.wikipedia.org/wiki/Anti-immunoglobulin

   This is a recombinant monoclonal antibody to human IgG. It has the ability to bind to all 4 human IgG subtypes: IgG1, IgG2, IgG3, and IgG4. [7] Anti-Human IgG [8E11] This is a recombinant monoclonal antibody to human IgG. However, it can screen for IgG in nonhuman primates including vervets, chimpanzees, and mangabeys.

5. Fragment crystallizable region - Wikipedia

   en.wikipedia.org/wiki/Fragment_crystallizable_region

   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.

6. Immunoglobulin class switching - Wikipedia

   en.wikipedia.org/wiki/Immunoglobulin_class_switching

   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]

7. Classical complement pathway - Wikipedia

   en.wikipedia.org/wiki/Classical_complement_pathway

   This process involves creating synthetic peptides that target conserved regions in HIV specific proteins and induce an antibody specific immune response through IgG antibodies. This is important for targeting the virus in its intracellular phase because the antibodies specific to the synthetic peptides can trigger the classical complement ...

8. Immunofluorescence - Wikipedia

   en.wikipedia.org/wiki/Immunofluorescence

   Photomicrograph of a histological section of human skin prepared for direct immunofluorescence using an anti-IgG antibody. The skin is from a patient with systemic lupus erythematosus and shows IgG deposit at two different places: The first is a band-like deposit along the epidermal basement membrane ("lupus band test" is positive).

9. Complementarity-determining region - Wikipedia

   en.wikipedia.org/wiki/Complementarity...

   The "upper" part of an antibody.The complementarity-determining regions of the heavy chain are shown in red (. Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively.