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FPLC purification of his-tagged proteins—TALON Superflow Metal Affinity Resin

TALON his-tag purification resin lets you prepare exceptionally pure his-tagged proteins from bacterial, mammalian, yeast, and baculovirus-infected cells, under native or denaturing conditions. TALON is an immobilized metal affinity chromatography (IMAC) resin charged with cobalt, which binds to his-tagged proteins with higher specificity than nickel-charged resins. As a result, TALON resin delivers his-tagged proteins of the highest purity. In addition, each cobalt ion is bound to the resin at four sites, resulting in low metal-ion leakage.

Reactive core contains cobalt for highest purity

TALON Superflow Metal Affinity Resin is complexed with cobalt ions that make it highly selective for his-tagged proteins. TALON’s cobalt-containing reactive core has strict spatial requirements—only proteins containing adjacent histidines or specially positioned, neighboring histidines are able to bind. The spatial requirements for nickel-based resins (e.g., Ni-NTA) are less strict—these resins have a much higher affinity for randomly positioned (i.e., non-his-tag) histidines. As a result, TALON resin binds more specifically to his-tagged proteins.

TALON Superflow Metal Affinity Resin is specifically designed for quick and effective purification of his-tagged proteins at high flow rates and medium pressure (up to 150 psi)—it’s ideal for FPLC applications. For prepacked 1 ml and 5 ml cartridges, please see the HisTALON Superflow Cartridge product page.

Uniform matrix guarantees less contamination

Cobalt-based resins have a more uniform structure than nickel-based resins. TALON resin contains negatively charged reactive sites that form three-dimensional pockets. Each pocket contains three carboxyl groups and one nitrogen atom that collectively bind a single, positively charged cobalt ion—an arrangement that allows the cobalt ion to bind to two adjacent histidine residues. In this configuration, cobalt is bound very tightly and does not leach out of the resin. Nickel-based resins are less homogeneous in structure because nickel ions can form two different coordination complexes: one of which forms a three-dimensional pocket similar to that of the TALON ligand, and a second that forms a planar (flat) structure. In the distorted, planar structure, each nickel ion binds to only two carboxyl groups and one nitrogen atom. As a result, the planar structure binds the nickel ions less tightly, allowing them to leach from the resin. TALON Metal Affinity Resin, with its uniform matrix, provides high affinity binding under a variety of purification conditions, ensuring optimal protein purification.

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Cat. #	Product	Size
635670	TALON® Superflow Metal Affinity Resin	250 mL	USD $2553.00
Cobalt-based immobilized metal affinity chromatography (IMAC) resin for the purification of recombinant his-tagged biomolecules under native or denaturing conditions. This resin permits one-step purification of his-tagged biomolecules under medium flow rates and pressures (up to 150 p.s.i.) for production-scale applications. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back FPLC purification of 6xHis-GFPuv with TALON Superflow FPLC purification of 6xHis-GFPuv with TALON Superflow. Nickel-NTA (Panel A) requires longer washing and lower flow rates to purify 6xHis- GFPuv than TALON Superflow Resin (Panel B). Protein was extracted in 50 mM sodium phosphate, 0.3 M NaCl, pH 7.0. Panel A.3.2 ml culture filtrate was loaded at 0.5 ml/min. Then nonadsorbed material was washed in the same buffer with 10 mM imidazole. Protein was eluted with 20 mM imidazole (Peak II) and 250 mM imidazole (Peak III). Panel B.3.2 ml culture filtrate was loaded at 1 ml/min. Then, nonadsorbed material was washed with the same extraction buffer and eluted with 150 mM imidazole (Peak II). Back SDS-PAGE of TALON CellThru Resin purified proteins SDS-PAGE of TALON CellThru Resin purified proteins. E. coli BL21 cells were sonicated in TALON wash buffer and run through a TALON CellThru column eluted in 150 mM imidazole. Note that some target protein is trapped in membrane fractions and does not get absorbed on the column. M: molecular weight marker. Back Native vs. denaturing purification procedures using TALON resin Native vs. denaturing purification procedures using TALON resin. Back Native purification with TALON resin preserves biological activity of proteins Native purification with TALON resin preserves 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 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 Resin. Back Purification of 6xHis-GFPuv under denaturing conditions using TALON resin 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. Back Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol 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 Back Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xHis 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. Back SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification $SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification$ SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification. Purification with TALON Superflow resin requires less washing with exceptional results. . Back 635670: TALON Superflow Metal Affinity Resin
635669	TALON® Superflow Metal Affinity Resin	2 x 250 mL	USD $4336.00
TALON Superflow Metal Affinity Resin is a cobalt-based immobilized metal affinity chromatography (IMAC) resin for the purification of recombinant his-tagged biomolecules under native or denaturing conditions. This resin permits one-step purification of his-tagged biomolecules under medium flow rates and pressures (up to 150 p.s.i.) for production-scale applications. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back FPLC purification of 6xHis-GFPuv with TALON Superflow FPLC purification of 6xHis-GFPuv with TALON Superflow. Nickel-NTA (Panel A) requires longer washing and lower flow rates to purify 6xHis- GFPuv than TALON Superflow Resin (Panel B). Protein was extracted in 50 mM sodium phosphate, 0.3 M NaCl, pH 7.0. Panel A.3.2 ml culture filtrate was loaded at 0.5 ml/min. Then nonadsorbed material was washed in the same buffer with 10 mM imidazole. Protein was eluted with 20 mM imidazole (Peak II) and 250 mM imidazole (Peak III). Panel B.3.2 ml culture filtrate was loaded at 1 ml/min. Then, nonadsorbed material was washed with the same extraction buffer and eluted with 150 mM imidazole (Peak II). Back SDS-PAGE of TALON CellThru Resin purified proteins SDS-PAGE of TALON CellThru Resin purified proteins. E. coli BL21 cells were sonicated in TALON wash buffer and run through a TALON CellThru column eluted in 150 mM imidazole. Note that some target protein is trapped in membrane fractions and does not get absorbed on the column. M: molecular weight marker. Back Native vs. denaturing purification procedures using TALON resin Native vs. denaturing purification procedures using TALON resin. Back Native purification with TALON resin preserves biological activity of proteins Native purification with TALON resin preserves 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 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 Resin. Back Purification of 6xHis-GFPuv under denaturing conditions using TALON resin 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. Back Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol 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 Back Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xHis 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. Back SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification $SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification$ SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification. Purification with TALON Superflow resin requires less washing with exceptional results. . Back 635669: TALON Superflow Metal Affinity Resin
635668	TALON® Superflow Metal Affinity Resin	4 x 250 mL	USD $7558.00
TALON Superflow Metal Affinity Resin is a cobalt-based immobilized metal affinity chromatography (IMAC) resin for the purification of recombinant his-tagged biomolecules under native or denaturing conditions. This resin permits one-step purification of his-tagged biomolecules under medium flow rates and pressures (up to 150 p.s.i.) for production-scale applications. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back FPLC purification of 6xHis-GFPuv with TALON Superflow FPLC purification of 6xHis-GFPuv with TALON Superflow. Nickel-NTA (Panel A) requires longer washing and lower flow rates to purify 6xHis- GFPuv than TALON Superflow Resin (Panel B). Protein was extracted in 50 mM sodium phosphate, 0.3 M NaCl, pH 7.0. Panel A.3.2 ml culture filtrate was loaded at 0.5 ml/min. Then nonadsorbed material was washed in the same buffer with 10 mM imidazole. Protein was eluted with 20 mM imidazole (Peak II) and 250 mM imidazole (Peak III). Panel B.3.2 ml culture filtrate was loaded at 1 ml/min. Then, nonadsorbed material was washed with the same extraction buffer and eluted with 150 mM imidazole (Peak II). Back SDS-PAGE of TALON CellThru Resin purified proteins SDS-PAGE of TALON CellThru Resin purified proteins. E. coli BL21 cells were sonicated in TALON wash buffer and run through a TALON CellThru column eluted in 150 mM imidazole. Note that some target protein is trapped in membrane fractions and does not get absorbed on the column. M: molecular weight marker. Back Native vs. denaturing purification procedures using TALON resin Native vs. denaturing purification procedures using TALON resin. Back Native purification with TALON resin preserves biological activity of proteins Native purification with TALON resin preserves 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 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 Resin. Back Purification of 6xHis-GFPuv under denaturing conditions using TALON resin 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. Back Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol 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 Back Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xHis 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. Back SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification $SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification$ SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification. Purification with TALON Superflow resin requires less washing with exceptional results. . Back 635668: TALON Superflow Metal Affinity Resin
635507	TALON® Superflow Metal Affinity Resin	100 mL	USD $1137.00
Cobalt-based immobilized metal affinity chromatography (IMAC) resin for the purification of recombinant his-tagged biomolecules under native or denaturing conditions. This resin permits one-step purification of his-tagged biomolecules under medium flow rates and pressures (up to 150 p.s.i.) for production-scale applications. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back FPLC purification of 6xHis-GFPuv with TALON Superflow FPLC purification of 6xHis-GFPuv with TALON Superflow. Nickel-NTA (Panel A) requires longer washing and lower flow rates to purify 6xHis- GFPuv than TALON Superflow Resin (Panel B). Protein was extracted in 50 mM sodium phosphate, 0.3 M NaCl, pH 7.0. Panel A.3.2 ml culture filtrate was loaded at 0.5 ml/min. Then nonadsorbed material was washed in the same buffer with 10 mM imidazole. Protein was eluted with 20 mM imidazole (Peak II) and 250 mM imidazole (Peak III). Panel B.3.2 ml culture filtrate was loaded at 1 ml/min. Then, nonadsorbed material was washed with the same extraction buffer and eluted with 150 mM imidazole (Peak II). Back SDS-PAGE of TALON CellThru Resin purified proteins SDS-PAGE of TALON CellThru Resin purified proteins. E. coli BL21 cells were sonicated in TALON wash buffer and run through a TALON CellThru column eluted in 150 mM imidazole. Note that some target protein is trapped in membrane fractions and does not get absorbed on the column. M: molecular weight marker. Back Native vs. denaturing purification procedures using TALON resin Native vs. denaturing purification procedures using TALON resin. Back Native purification with TALON resin preserves biological activity of proteins Native purification with TALON resin preserves 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 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 Resin. Back Purification of 6xHis-GFPuv under denaturing conditions using TALON resin 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. Back Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol 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 Back Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xHis 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. Back SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification $SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification$ SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification. Purification with TALON Superflow resin requires less washing with exceptional results. . Back 635507: TALON Superflow Metal Affinity Resin
635506	TALON® Superflow Metal Affinity Resin	25 mL	USD $335.00
Cobalt-based immobilized metal affinity chromatography (IMAC) resin for the purification of recombinant his-tagged biomolecules under native or denaturing conditions. This resin permits one-step purification of his-tagged biomolecules under medium flow rates and pressures (up to 150 p.s.i.) for production-scale applications. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back FPLC purification of 6xHis-GFPuv with TALON Superflow FPLC purification of 6xHis-GFPuv with TALON Superflow. Nickel-NTA (Panel A) requires longer washing and lower flow rates to purify 6xHis- GFPuv than TALON Superflow Resin (Panel B). Protein was extracted in 50 mM sodium phosphate, 0.3 M NaCl, pH 7.0. Panel A.3.2 ml culture filtrate was loaded at 0.5 ml/min. Then nonadsorbed material was washed in the same buffer with 10 mM imidazole. Protein was eluted with 20 mM imidazole (Peak II) and 250 mM imidazole (Peak III). Panel B.3.2 ml culture filtrate was loaded at 1 ml/min. Then, nonadsorbed material was washed with the same extraction buffer and eluted with 150 mM imidazole (Peak II). Back SDS-PAGE of TALON CellThru Resin purified proteins SDS-PAGE of TALON CellThru Resin purified proteins. E. coli BL21 cells were sonicated in TALON wash buffer and run through a TALON CellThru column eluted in 150 mM imidazole. Note that some target protein is trapped in membrane fractions and does not get absorbed on the column. M: molecular weight marker. Back Native vs. denaturing purification procedures using TALON resin Native vs. denaturing purification procedures using TALON resin. Back Native purification with TALON resin preserves biological activity of proteins Native purification with TALON resin preserves 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 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 Resin. Back Purification of 6xHis-GFPuv under denaturing conditions using TALON resin 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. Back Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol 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 Back Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin. N-terminal 6xHis 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. Back SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification $SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification$ SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification. Purification with TALON Superflow resin requires less washing with exceptional results. . Back 635506: TALON Superflow Metal Affinity Resin

Overview

Choice of native or denaturing purification conditions

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. Deciding whether to use native or denaturing purification conditions depends on protein location, solubility, accessibility of the his tag, downstream applications, and preservation of biological activity.

Native conditions
Purifying a protein under native conditions is the most efficient way to preserve its biological activity, but requires that the protein be 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

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—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 his tag
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 provides higher yields than Ni-NTA in the presence of β-mercaptoethanol.

More Information

Features

Exhibits high affinity for his-tagged proteins
Ideal for FPLC applications
No copurification of proteins
Resists metal leakage
Performs well under a wide range of purification conditions

Applications

Purified recombinant his-tagged proteins can be used for:

Crystallography
Functional assays
Structural investigations
Other applications

Additional product information

Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.

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FPLC purification of his-tagged proteins—TALON Superflow Metal Affinity Resin

Reactive core contains cobalt for highest purity

Uniform matrix guarantees less contamination

Notice to purchaser

FPLC purification of 6xHis-GFPuv with TALON Superflow

SDS-PAGE of TALON CellThru Resin purified proteins

Native vs. denaturing purification procedures using TALON resin

Native purification with TALON resin preserves biological activity of proteins

Purification of 6xHis-GFPuv under denaturing conditions using TALON resin

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin

SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification

635670: TALON Superflow Metal Affinity Resin

Notice to purchaser

FPLC purification of 6xHis-GFPuv with TALON Superflow

SDS-PAGE of TALON CellThru Resin purified proteins

Native vs. denaturing purification procedures using TALON resin

Native purification with TALON resin preserves biological activity of proteins

Purification of 6xHis-GFPuv under denaturing conditions using TALON resin

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin

SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification

635669: TALON Superflow Metal Affinity Resin

Notice to purchaser

FPLC purification of 6xHis-GFPuv with TALON Superflow

SDS-PAGE of TALON CellThru Resin purified proteins

Native vs. denaturing purification procedures using TALON resin

Native purification with TALON resin preserves biological activity of proteins

Purification of 6xHis-GFPuv under denaturing conditions using TALON resin

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin

SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification

635668: TALON Superflow Metal Affinity Resin

Notice to purchaser

FPLC purification of 6xHis-GFPuv with TALON Superflow

SDS-PAGE of TALON CellThru Resin purified proteins

Native vs. denaturing purification procedures using TALON resin

Native purification with TALON resin preserves biological activity of proteins

Purification of 6xHis-GFPuv under denaturing conditions using TALON resin

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin

SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification

635507: TALON Superflow Metal Affinity Resin

Notice to purchaser

FPLC purification of 6xHis-GFPuv with TALON Superflow

SDS-PAGE of TALON CellThru Resin purified proteins

Native vs. denaturing purification procedures using TALON resin

Native purification with TALON resin preserves biological activity of proteins

Purification of 6xHis-GFPuv under denaturing conditions using TALON resin

Native purification of 6xHis protein using TALON resin in the presence of beta-mercaptoethanol

Protein purification yields in the presence of beta-mercaptoethanol with TALON resin compared to Ni-NTA resin

SDS-PAGE of FPLC fractions from 6xHis-GFPuv purification

635506: TALON Superflow Metal Affinity Resin

Overview

Choice of native or denaturing purification conditions

Use of reducing agents

More Information

Features

Applications

Additional product information