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
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 M (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
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