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Affinity capture surfaces
Affinity capture is based on the specific binding of a tagged biomolecule to its receptor. The plate surface is therefore developed with one of the binding pair (the receptor) immobilized on its surface, while the tag is linked to a biomolecule either by chemical coupling or genetic engineering. The tagged biomolecule can then be captured on the plate surface with a high degree of specificity.
Surface characteristics
- Affinity tagged biomolecules have highly specific binding
- Reduced variability in molecular orientation
- Immobilizer surfaces improve S/N ratios
- Streptavidin biotin interaction can be exploited to immobilize a wide range of biomolecules (proteins, peptides, haptens, nucleic acids)
| Biomolecule | Surface type | Key features |
|---|---|---|
| Antibody-Binding Plates | Secondary antibody | Our antibody-coated platesare useful for binding assays when available antibodies are in low quantities, denatured, and become inactive upon direct adsorption to polystyrene plates. |
| Biotin-Binding Plates | Streptavidin | Streptavidin- and NeutrAvidin-coated plates for binding biotinylated antibodies or probes for ELISA and other target-specific assays. Biotin-binding plates are ideal for applications when direct adsorption to polystyrene denatures antibodies or the target molecule. |
| GST-Binding Plates | Glutathione | Coated with intact glutathione (GSH) for use in capture and detection assays involving glutathione-S-transferase (GST) fusion proteins. |
| Nickel Chelate/Copper Chelate | Nickel and copper chelate–coated plates are ideal for analyzing polyhistidine-tagged fusion proteins by ELISA-based methods. |
Resources
For Research Use Only. Not for use in diagnostic procedures.