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Once the solid substrate bead technology has been chosen, antibodies are coupled to the beads and the antibody-coated-beads can be added to the heterogeneous protein sample (e.g. homogenized tissue). At this point, antibodies that are immobilized to the beads will bind to the proteins that they specifically recognize.
Dynabeads may be covalently linked to an antibody that recognizes a specific protein on the surface of the target cell-type. Alternatively, Dynabeads may attach to the cell indirectly, either via streptavidin on the Dynabead linking to a biotinylated primary antibody , or a secondary antibody on the Dynabead linking to the primary antibody.
Protein G is an immunoglobulin-binding protein expressed in group C and G streptococcal bacteria much like protein A but with differing binding specificities. It is a ~60-kDA (65 kDA for strain G148 and 58 kDa for strain C40) [1] cell surface protein that has found application in purifying antibodies through its binding to the Fab and Fc region.
Subsequently, the tagged protein (with its binding partners) is retrieved using an affinity selection process. The first type of bead added is coated with Immunoglobulin G, which binds to the TAP tag's outermost end. The beads, with the proteins of interest, are separated from the lysate via centrifugation.
The first example of protein A being coupled to a porous bead for purification of IgG was published in 1972. [19] Immunoprecipitation studies with protein A conjugated to beads are also commonly used to purify proteins or protein complexes indirectly through antibodies against the protein or protein complex of interest.
The protein can then be covalently coupled to a solid support such as agarose and used as an affinity ligand in purifications of antibody from immune serum. For thoroughness, the GST protein and the GST-fusion protein can each be coupled separately. The serum is initially allowed to bind to the GST affinity matrix.
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