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  • Video: Capturem his maxiprep
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  • Visual protocol: Capturem his maxiprep
  • Visual protocol: Capturem his miniprep
  • Capturem nickel column reagent compatibility
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  • TALON: Native vs denaturing purification
  • Protocol: denaturing purification with TALON resin, imidazole elution
  • Protocol: native purification with TALON resin, imidazole elution
  • Protocol: native purification with TALON resin, pH elution
Selection guides TALON selection guide
Home › Learning centers › Protein research › His-tag purification › Protocols › TALON: Native vs denaturing purification

His-tag purification

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    • Video: Capturem his maxiprep
    • Video: Capturem his miniprep
    • Visual protocol: Capturem his maxiprep
    • Visual protocol: Capturem his miniprep
    • Capturem nickel column reagent compatibility
    • TALON reagent compatibility
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    • TALON: Native vs denaturing purification
    • Protocol: denaturing purification with TALON resin, imidazole elution
    • Protocol: native purification with TALON resin, imidazole elution
    • Protocol: native purification with TALON resin, pH elution
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Selection guides TALON selection guide

Choice of native or denaturing purification conditions and use of reducing agents with TALON resin

Native or denaturing?—Selecting the right purification conditions

Deciding whether to use native or denaturing purification conditions depends on protein localization, solubility, accessibility of the histidine tag, downstream applications, and whether preservation of biological activity is required. TALON resin retains its protein-binding specificity and yield under a variety of purification conditions. It is stable under both denaturing and native (nondenaturing) conditions.

TALON resin can be used for either native or denaturing purifications.

Native conditions

Purifying a protein under native conditions (see example below) is the most efficient way to preserve its biological activity, but requires that the protein is soluble. Advantages include:

  • Eliminating the renaturation step at the end of the purification, saving time, and preventing significant loss of activity
  • Retaining the ability to copurify enzyme subunits, cofactors, and associated proteins

Purification of a his-tagged protein under native conditions.

Native purification with TALON resin preserves the biological activity of proteins. Fresh cells (0.5 g) expressing 6xHis GFPuv were extracted in 5 ml of 50 mM sodium phosphate; 0.3 M NaCl, pH 7.0 Panel A. Elution profile of GFP which was loaded, washed with the same buffer, and then eluted with a step gradient of imidazole (150 mM). Panel B. Fractions were analyzed by SDS-PAGE. The fluorescent signal of green fluorescent protein (GFPuv) was completely enriched by TALON Superflow Metal Affinity Resin.

Denaturing conditions

Because proteins that are overexpressed in prokaryotic systems sometimes form insoluble aggregates called inclusion bodies, you may need to purify proteins under denaturing conditions (see example below)—using strong denaturants such as 6 M guanidinium or 8 M urea to enhance protein solubility. Advantages include:

  • Complete solubilization of inclusion bodies and his-tagged proteins
  • Improved binding to the matrix and reduced nonspecific binding, due to full exposure of the tag

Purification of a his-tagged protein with 8 M urea buffers for a denaturing purification.

Purification of 6xHis GFPuv under denaturing conditions using TALON resin. The fusion protein was purified in 8 M urea using TALON resin. M = molecular weight markers.

His-tagged proteins purified under denaturing conditions can be used directly in subsequent applications or may need to be renatured and refolded. Protein renaturation and refolding can be performed prior to elution from the column. However, yields of recombinant proteins will be lower than under native conditions, because urea and guanidinium molecules compete with histidines for binding to metal.

Use of reducing agents

Purification with TALON resin may be carried out in the presence of β-mercaptoethanol, but not DTT or DTE, to preserve reduced sulfhydryl (-SH) groups that are important for the biological activity and structure of a given protein.

TALON resin provides exceptional purification even in the presence of BME.

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol. N-terminal 6xhis-tagged mouse DHFR (19.5 kDa) was expressed in E. coli. 2 ml of lysate was purified using gravity flow on TALON resin in increasing concentrations of beta-mercaptoethanol. Even lanes: 20 μl of nonadsorbed material. Odd lanes: 5 μl of eluate.

TALON provides higher yields than Ni-NTA in the presence of β-mercaptoethanol.

Protein yields for purifications containing BME are better for TALON than Ni-NTA protocols.

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xhis-tagged DHFR was expressed and purified under native conditions. Protein concentrations were determined by Bradford assay. Yields are expressed as a percentage of total protein in the cell lysate.


TALON resin application protocols

Denaturing purification

Choose between mini-scale purification, batch/gravity-flow column purification, and large-scale purification protocols.

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