JoVE Encyclopedia of Experiments
Microbiology
0 views • 2:54 min • November 28th, 2025
This article describes a method for purifying polyhistidine-tagged proteins from bacterial cells. The process involves sonication, centrifugation, and nickel-based affinity chromatography to isolate the target protein efficiently.
Affinity chromatography using nickel-based resins enables rapid, selective purification of recombinant proteins, supporting early-stage target validation and assay development in biopharma R&D. Reliable isolation of polyhistidine-tagged proteins ensures consistent reagent quality for downstream screening and mechanistic studies. This workflow underpins reproducibility and scalability across discovery and preclinical research pipelines.
This affinity purification method is positioned at the interface of early discovery and assay development, enabling seamless transition to preclinical research when recombinant protein reagents are required.
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Last updated: 1 August 2026