- Purification methods overview
- TALON resin selection guide
- Selection guide: His60 resin
- xTractor Buffer is optimized for superior protein yield
- Why tag a protein?
- Tech note: cobalt resin
- Simplified purification of active, secreted his-tagged proteins
- Overview: His60
- Tech note: Capturem technology
- Tech note: Capturem large volume
- Magnetic beads
- FAQs: TALON
- 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
- His60 reagent compatibility
- 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
TALON reagent compatibility
TALON 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.
|Reagents compatible with TALON Resin|
|Beta-mercaptoethanola||10 mM (with caution)|
|CHAPSb||1% (with caution)|
|Guanidine hydrochloridea||6 mM|
|Imidazoled||200 mM at pH 7.0-8.0, for elution|
|SDSb||1% with caution|
- Use resin immediately after equilibrating with buffers containing these reagents. Otherwise, the resin will change color. Do not store resin in buffers containing these reagents.
- Ionic detergents like CHAPS (3-[(3-Cholamidopropyl)-dimethylammonio]-1-propane-sulfonate), SDS (sodium dodecyl sulfate), and sarkosyl are compatible up to 1%. However, due to their charged nature, you should anticipate interference with binding, even at low concentrations.
- Ethanol may precipitate proteins, causing low yields and column clogging.
- Imidazole cannot be used at concentrations higher than 5–10 mM for loading his-tagged proteins, because it competes with the histidine side chains (imidazole groups) for binding to the immobilized metal ions.
- Tris coordinates weakly with metal ions, causing a decrease in capacity.
|Reagents incompatible with TALON Resin|
|These reagents are incompatible at any concentration:|
Takara Bio USA, Inc.
United States/Canada: +1.800.662.2566 • Asia Pacific: +1.650.919.7300 • Europe: +33.(0)1.3904.6880 • Japan: +81.(0)77.565.6999
FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES. © 2023 Takara Bio Inc. All Rights Reserved. All trademarks are the property of Takara Bio Inc. or its affiliate(s) in the U.S. and/or other countries or their respective owners. Certain trademarks may not be registered in all jurisdictions. Additional product, intellectual property, and restricted use information is available at takarabio.com.