Monoclonal Anti-Human IgG (mouse IgG2a isotype) is derived from the hybridoma1 produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Immunoglobulins (Igs) belongs immunoglobulin super-family and have two heavy (H) and two light (L) chain, held together by disulphide linkages. The four classes of IgG can be IgG1, IgG2, IgG3 and IgG4. Each light chain comprises one variable N-terminal region and a constant C-terminal region. Heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal region.
The antibody is specific for the Fc portion of human IgG and recognizes an epitope common to all human IgG subclasses. This antibody was adopted as an Fc specific reagent in the IUIS/WHO study.
Monoclonal Anti-Human IgG (Fc specific) antibody produced in mouse has been used in:
- enzyme linked immunosorbent assay (ELISA)
- imprint immunofixation (IIF)
- immunofluorometric assay (IFMA)
- hemagglutination (HA)
- hemagglutination inhibition (HAI)
- particle counting immunoassay(PACIA)
0.2, 0.5 mL in glass bottle
Although the antibody site is located in the terminal end of human IgG (part of the Fab fragment), the Fc portion has various important functions such as complement fixation, site for rheumatoid factor (autoantibody directed to Fc) attachment, passage through the placental membrane and protein A binding. A certain population of lymphocytes also possess a "Fc receptor". These functions indicate the importance of immunoreagents specific for the Fc fragment of human IgG.
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