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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.
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.
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.
Suspension array technology (or SAT) is a high throughput, large-scale, and multiplexed screening platform used in molecular biology.SAT has been widely applied to genomic and proteomic research, such as single nucleotide polymorphism (SNP) genotyping, genetic disease screening, gene expression profiling, screening drug discovery and clinical diagnosis.
Proteins and protein complexes can be separated; e.g., in immunoprecipitation protocols. Molecular studies and diagnostics also benefit from microbeads (e.g. immunoassay IVD and nucleic acid IVD). When microbeads are coupled with streptavidin , they offer a very efficient way to isolate any biotinylated molecule.
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.
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