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IMAC


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WorkBeads IMAC

The WorkBeads™ IMAC media for Immobilized Metal Ion Affinity Chromatography (IMAC) can successfully be used for easy and convenient purification of polyhistidine-tagged (His-tagged) proteins in both biotechnology research, method development and industrial purification of proteins. The high porosity of the base matrix facilitates optimal protein interaction.

WorkBeads IMAC media are based on cross-linked agarose with chelating ligands based on nitrilotriacetic acid (NTA), iminodiacetic acid (IDA) or tris(2-aminoethyl)amine (TREN). The media are available as both pre-charged and uncharged WorkBeads NTA or WorkBeads IDA, and uncharged WorkBeads TREN. The pre-charged media contains WorkBeads NTA or WorkBeads IDA with metal ions:  Ni2+, Co2+, Cu2+ or Zn2+, which are immobilized on the media via the chelating ligand.

The uncharged WorkBeads IMAC media can be charged with several of the divalent and trivalent transition metal ions (e.g., Ni2+, Co2+, Cu2+ or Zn2+, Fe3+ or Ga3+), for purification of polyhistidine-tagged proteins or other metal ion binding proteins. Media charged with Fe3+ and Ga3+ ions may be used for purification of phosphorylated peptides and proteins. The IMAC media can also be used in their uncharged state for removal of the above mentioned metal ions from solution.


 - WorkBeads 40 NTA
 - WorkBeads 40 Ni-NTA
 - WorkBeads 40 Co-NTA
 - WorkBeads 40 Cu-NTA
 - WorkBeads 40 Zn-NTA
 - WorkBeads 40 IDA
 - WorkBeads 40 Ni-IDA
 - WorkBeads 40 Co-IDA
 - WorkBeads 40 Cu-IDA
 - WorkBeads 40 Zn-IDA
 - WorkBeads 40 TREN
 

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