Anti-Rabbit IgG is developed in goat using rabbit IgG isolated from normal rabbit serum as the immunogen. IgG is present in large quantities in the human serum. It constitutes about 10-20% of the plasma proteins. IgG is composed of glycoproteins, out of which it is 82-96% proteins and 4-18% carbohydrates. It consists of four sub-classes i.e IgG1, IgG2, IgG3, and IgG4. IgG is composed of four polypeptide chains-two heavy chains (γchains) and two light chains (κ or λ chains) which are linked by inter-chain disulfide bonds. The heavy chains consist of a N-terminal variable domain (VH) and three constant domains (CH1, CH2, CH3). A hinge region exists between the CH1 and CH2 region. The light chains have one N-terminal variable domain (VL) and one constant domain (CL). The heavy and the light chains are linked at VH and CH1 domain to form the Fab arm (Fragment antigen binding). The antigen binds to the V regions of the antibody.
Anti-Rabbit IgG (whole molecule) antibody produced in goat was used for immunohistochemistry of rat brain sections. It was also used in protein spotting assays.
Acciones bioquímicas o fisiológicas
IgG is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections.
Nota de preparación
treated to remove lipoproteins
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