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This gene encodes a glycoprotein with an approximate molecular weight of 76.5 kDa. It is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of this protein is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocy

Fluorescein is a fluorophore commonly used to label proteins - protein-fluorescein conjugates are not usually susceptible to precipitation. In addition to its relatively high absorptivity, excellent fluorescence quantum yield and good water solubility, fluorescein has an excitation maximum of 494 nm that closely matches the 488 nm spectral line of the argon-ion laser, making it an important fluorophore for confocal laser-scanning microscopy and flow cytometry applications. Its fluorescence is

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

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

IgE is the least abundant immunoglobulin in plasma, found at a concentration of less that 0.6 micrograms/ml of normal plasma. Elevated IgE levels are found in patients experiencing severe allergic reactions and parasitic infections. In a myeloma condition, IgE is produced by a single clone of plasma cells. The structure of myeloma IgE, however, is normal, and the immunoglobulin purified from a myeloma source is a useful protein for studying immunoglobulin behavior. The affinity purified IgE r