Metal Affinity Resin
Metal Affinity Resin - Related Videos
05:35
Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
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Cited by 5 •
2020
We present an assay for easy quantification of metals introduced to samples prepared using immobilized metal affinity chromatography. The method uses hydroxynaphthol blue as the colorimetric metal indicator and a UV-Vis spectrophotometer as the detector.
02:38
Anion Exchange Resin–Based Detection of Viruses from Bioaerosols
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2026
Source: Schaeffer, J. W., Chandler, et al. Detection of Viruses from Bioaerosols Using Anion Exchange Resin. J. Vis. Exp. (2018).This video demonstrates the detection of viruses from bioaerosols using an anion exchange resin. A liquid impinger containing the resin is used to capture viruses from the air. The resin is collected and treated with a virus lysis buffer containing carrier RNA. The lysate is transferred to a microcentrifuge tube for viral RNA isolation, followed by qRT-PCR to amplify...
07:51
Acrylic Resin Molding Based Head Fixation Technique in Rodents
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Cited by 4 •
2016
Traditional head fixation techniques have used metallic frames attached on the skull as an interface for head fixation apparatus. This protocol demonstrates a frameless, acrylic resin molding based head fixation technique for behavioral tasks in rodents.
08:46
Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
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Cited by 48 •
2014
Antifreeze proteins (AFPs) bind to specific planes of ice to prevent or slow ice growth. Fluorescence-based ice plane affinity (FIPA) analysis is a modification of the original ice-etching method for determination of AFP-bound ice planes. AFPs are fluorescently labeled, incorporated into macroscopic single ice crystals, and visualized under UV light.
03:41
DFE-Based Affinity Chromatography: A Technique for Purification of 2F5 Monoclonal Antibodies from a Crude Sample Using High Ionic Strength-Based Elution Conditions
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2025
This video describes an affinity chromatography technique for purifying 2F5 monoclonal antibodies using the DsRed-2F5-Epitope or DFE ligands. The purified 2F5 monoclonal antibodies are essential drugs in immunotherapy.
FAQs
The immobilized metal ions coordinate with electron-donating groups on biomolecules, particularly histidine residues in engineered polyhistidine tags. This interaction gives tagged proteins a selective binding advantage when they are mixed with complex biological material. The resulting selectivity helps distinguish a recombinant target from many other components in a cell lysate.
Polyhistidine tags provide multiple histidine residues that can interact with the immobilized metal center. Their engineered placement on a recombinant protein creates a recognition feature that the resin can exploit during purification. This strategy improves recovery of the intended protein from a complex lysate and supports subsequent structural, biochemical, or functional studies.
Imidazole promotes elution by competing with histidine-containing interactions at the immobilized metal site. As imidazole is added, the target protein becomes less strongly retained and can be recovered from the resin. Changing pH provides another release mechanism by altering the coordination environment, allowing researchers to select an elution approach suited to the sample.
Selectivity depends mainly on the interaction between the immobilized metal ion and electron-donating groups, especially those supplied by a polyhistidine tag. The composition of the starting material also matters because purification commonly begins with a complex cell lysate. These factors determine how effectively the tagged target is distinguished from unrelated biomolecules.
A typical workflow applies a cell lysate to the resin so the tagged protein can bind, separates unbound material, and then releases the retained protein with imidazole or a pH change. This sequence concentrates the target while reducing unrelated lysate components, producing a preparation suitable for later structural, biochemical, or functional analysis.
This approach is useful when researchers need to isolate a recombinant protein from a complex cell lysate. The purified material can support structural studies, biochemical experiments, and functional investigations. Because the method also enables sample concentration, it can help prepare a target for analyses that require a more enriched or concentrated protein preparation.
Metal affinity resin is available in reusable formats and is compatible with automated workflows. Those characteristics allow the same purification principle to fit routine laboratory processing as well as more organized or repeated sample preparation. In biotechnology and protein research, this can streamline recovery of tagged recombinant proteins for downstream structural, biochemical, or functional work.