TALON® Magnetic Beads Buffer Kit, 635638, Takara Bio Inc (CAT#: STEM-C-3845-LGZ)

Combine the advantages of our highly selective TALON chemistry and magnetic bead separation. When placed on a magnetic separator, the magnetic particles in the beads help separate minute amounts of proteins quickly and easily. Beads pre-filled with Co2+ have higher specificity for His-tagged proteins compared to nickel-based resins. Co2+ is bound to the beads using TALON's unique tetradentate metal chelator, which binds cobalt at four sites, virtually eliminating metal leakage during purification.

Highly specific binding and elution
TALON magnetic beads bind low to high molecular weight his-tagged proteins with high specificity. Purified proteins were eluted in small volumes (50-200 μl), resulting in concentrated samples (up to 3 mg/ml). TALON Magnetic Beads are supplied as a 5% suspension with a binding capacity of 750µg of protein per mL of suspension.

Micro-scale screening
Microscale purification using TALON magnetic beads can be used for screening expression levels or protein-protein interaction studies. Additionally, the use of TALON chemistry allows seamless scaling up of the purification of target proteins using our standard TALON resins.

Choice of native or denaturing purification conditions
TALON resin maintains its protein binding specificity and yield under a variety of purification conditions. It is stable under both denaturing and native (non-denaturing) conditions. Deciding whether to use native or denaturing purification conditions depends on the protein's location, solubility, availability of the histidine tag, downstream applications, and preservation of biological activity.

local conditions

Purifying proteins under native conditions is the most effective way to maintain their biological activity, but requires the protein to be soluble. Advantages include:

The redenaturation step at the end of purification is eliminated, saving time and preventing significant loss of activity.
Retains the ability to co-purify enzyme subunits, cofactors, and associated proteins.

Denaturation conditions

Because proteins overexpressed in prokaryotic systems sometimes form insoluble aggregates called inclusion bodies, you may need to purify the protein under denaturing conditions - use strong denaturants such as 6M guanidine or 8M urea to enhance protein solubility. Advantages include:

Complete solubilization of inclusion bodies and his-tagged proteins.
Improves binding to the matrix and reduces non-specific binding because the histidine tag is fully exposed.
His-tagged proteins purified under denaturing conditions can be used directly for subsequent applications, or may require renaturation and refolding. Protein refolding and refolding can be performed prior to elution from the column. However, because urea and guanidine molecules compete with histidine for metal binding, the yield of recombinant protein will be lower than under native conditions.

Use of reducing agent

TALON resins can be purified in the presence of β-mercaptoethanol instead of DTT (dithiothreitol) or DTE (dithioerythritol) to preserve reductions that are important for the biological activity and structure of specific proteins Sulfhydryl (-SH) group. In the presence of β-mercaptoethanol, the yield of TALON was higher than that of Ni-NTA.

Size: Each

Choose from native or denaturing conditions to purify proteins
Directed display of 6xHis-tagged proteins improves reproducibility and signal-to-noise ratio
Different numbers of beads per well allow for a wide range of binding capacities
A powerful tool for analyzing interactions between biomolecules

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