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Protein Expression & Purification


Products >  Protein_Expression_and_Purification >  His-Tagged_Protein_Purification >  Cobalt_Columns-Spin

Fast, Small-Scale His-Tagged Protein Purification—TALON Spin Columns

TALON Spin Columns contain 0.5 ml of TALON-NX, an immobilized metal affinity chromatography resin for the purification of recombinant his-tagged proteins under native or denaturing conditions.

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 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.

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.

TALON Spin Columns

These ready-made spin columns contain TALON-NX Resin for the simultaneous purification of several his-tagged proteins in parallel in only 30 minutes. They are recommended for small-scale, single-use applications, such as verifying his-tagged protein expression in transformants, or trial-level purification protocols.

At-A-Glance Documents Images & Data Resources

Features

  • Exhibits high affinity for his-tagged proteins
  • No copurification of proteins
  • Resists metal leakage
  • Performs well under a wide range of purification conditions
  • Ready-to-use spin columns
  • Each column contains 0.5 ml of resin

Applications

  • His-tagged protein purification
  • Recombinant protein purification & identification
  • Spin column purification

Additional 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.


 
 
Products
Cat. # Product Package Size Price License # of Units Select
635601 TALON® Spin Columns 10 x 0.5 mL Columns $117.00 License Statements
635602 TALON® Spin Columns 25 x 0.5 mL Columns $227.00 License Statements
635603 TALON® Spin Columns 50 x 0.5 mL Columns $356.00 License Statements
 

 

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