Human IgGs are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. IgGs have four distinct isoforms, ranging from IgG1 to IgG4. These antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders,.
Antibody is isolated from anti-human IgG antiserum by immunospecific purification to remove essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fab fragment of human IgG. Anti-Human IgG is conjugated to peroxidase and then further purified to remove unconjugated material.
Fab fragment of human IgG
Anti-Human IgG (Fab specific)-Peroxidase antibody produced in goat has been used in:
- western blot
- direct enzyme linked immunosorbent assay (ELISA) at 1:40,000 dilution for analysis of yeast cultures genetically modified to produced recombinant Fab fragments.
- dot blot
- immunohistochemistry (formalin-fixed, paraffin-embedded sections, 1:200)
Anti-Human IgG antibody was used at a 1:10,000 dilution in PBS and incubated for 1 hour at room temperature. Binding in ELISA assays was detected with a O-phenylene-diamine substrate solution (Sigma).
Goat anti-human IgG (Fab specific)-peroxidase antibody can be used for direct ELISA (1:40,000), dot blot and immunohistochemistry (formalin-fixed, paraffin-embedded sections, 1:200) applications.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT
Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
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