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Immunoglobulin G (IgG), is one of the most abundant proteins in serum with normal levels between 8-17 mg/mL in adult blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions; to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombin

Immunoglobulin G (IgG), is one of the most abundant proteins in serum with normal levels between 8-17 mg/mL in adult blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions; to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombin

IgM normally constitutes about 10% of serum immunoglobulins. IgM antibody is prominent in early immune responses to most antigens and is largely confined to plasma due to it's large size. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. Due to it's high valency IgM is more efficient than other isotypes is binding antigens with repeating epitopes (virus particles and red blood cells) and is more efficient tha

Human IgG consists of four subclasses (1-4) that can be recognised by antigen differences in their heavy chains. Each subclass has different biological and physiochemical properties. The IgG subclass may be preferentially produced in response to different antigens.$nThe Fab fragment (fragment antigen binding) is the antigen region of the IgG molecule. It is composed of one constant and one variable domain of each of the heavy and the light chain.

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately