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-Mouse IgG (Fc specific)-Biotin antibody has been used in enzyme linked immunosorbent assay (ELISA), dot blot, immunohistology, nuclear labeling, ELISA-inhibition method. immunohistochemistry.
Anti-Mouse IgG (Fc specific)-Biotin antibody produced in goat was used for immunocytochemistry staining to visualize neonatal myosin in chicken muscle sections. It was used for ELISPOT analysis to study IgG levels in mice infected with cholera toxin.
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. The coupling of biotin to Anti-Mouse IgG (Fc specific) antibody allows for the binding of various labels such as avidin or streptavidin.
Antibody adsorbed with human IgG and rat serum proteins.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Adsorbed to reduce background staining with human or rat samples.
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