direct immunofluorescence: 1:100 using human peripheral blood immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using human tonsils
IgG is present in large quantities in the human serum. 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 (γ chains) 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.
Application
Anti-Rat IgG (whole molecule)-TRITC antibody has been used in
confocal microscopy
immunohistochemistry
immunofluorescence
Biochem/physiol Actions
IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It 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.
IgG, a monoclonal antibody can be cleaved at the hinge region by nonspecific proteases like papain and pepsin. This can result in univalent Fab (Fragment antigen binding) fragments or bivalent F(ab′)2 fragments. These two enzymes have a broad substrate specificity resulting in heterogenous fragments.
Other Notes
Antibody adsorbed with human IgG.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
Adsorbed to reduce background staining with human samples.
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