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)
BiomoleculeSurface typeKey features
Antibody-Binding PlatesSecondary antibodyOur 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 PlatesGlutathioneCoated with intact glutathione (GSH) for use in capture and detection assays involving glutathione-S-transferase (GST) fusion proteins.

His Tag-Binding Plates

Nickel Chelate/Copper ChelateNickel 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.