Zymography
Zymography detects protease activity in protein samples by electrophoresis through a substrate-containing polyacrylamide gel followed by renaturation and substrate digestion.
Co-Immunoprecipitation (Co-IP)
Co-immunoprecipitation is an antibody-based method for isolating a target protein along with its interacting partners from a complex biological lysate.
Dialysis, Ultrafiltration, and Buffer Exchange
Dialysis, ultrafiltration, and buffer exchange are essential protein handling techniques for changing buffer composition, removing small molecules, or concentrating samples.
Native PAGE and Zymography
Native PAGE separates proteins in their folded, functional state, while zymography detects enzyme activity directly within an electrophoretic gel.
Surface Plasmon Resonance (SPR)
Surface plasmon resonance is a label-free optical technique for measuring real-time biomolecular interactions and binding kinetics.
Affinity Capture
Affinity capture is a set of biochemical techniques that purify or isolate proteins by exploiting specific binding interactions between a tagged or native protein and an immobilized capture reagent.
Biotin-Avidin Systems
Biotin-avidin systems exploit the strongest known non-covalent biological interaction to label, capture, and detect biomolecules in biochemical assays.
GST-Tag Pull-Down
GST-tag pull-down uses glutathione S-transferase fusion proteins immobilized on glutathione agarose to purify recombinant proteins or capture interacting partners.
His-Tag / IMAC Purification
Immobilized metal affinity chromatography purifies polyhistidine-tagged recombinant proteins using immobilized metal ions and imidazole elution.
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