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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

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

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

Fraction V bovine serum albumin. Albumin is one of the most extensively utilized proteins in the medical industry. Its availability, inherent stability, and ligand binding ability make albumin an essential component in the production of many therapeutic drugs, vaccines and diagnostic tests. Albumin is a soluble, monomeric protein which comprises about one half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and pla

In chickens, immunoglobulin Y is the functional equivalent to Immunoglobulin G (IgG). Like IgG, it is composed of two light and two heavy chains. Structurally, these two types of immunoglobulin differ primarily in the heavy chains, which in IgY have a molecular mass of about 65,100 atomic mass units (amu), and are thus larger than in IgG. The light chains in IgY, with a molar mass of about 18,700 amu, are somewhat smaller than the light chains in IgG. The molar mass of IgY thus amounts to abo

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