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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

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

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

Monomeric IgA constitutes 5-15 % of the serum immunoglobulins whereas dimeric IgA is localized to mucosa surfaces such as saliva, gastrointestinal secretion, bronchial fluids and milk. Mucosal IgA plays a major role in host defence by neutralising infectious agents at mucosal surfaces. The production is usually local and antigen specific IgA producing B-cells can be found in regions under the lamina propria where they mature into dimeric IgA producing plasma cells. IgA deficiency is the most