Product category:
Chromatography accessories
News Release from: Harvard Apparatus | Subject: SpinColumns
Edited by the Laboratorytalk Editorial
Team on 09 August 2005
Imac useful for recombinant proteins and
peptides
Immobilised metal ion affinity chromatography (Imac) is based on the specific coordinate covalent binding between histidine or other metal binding amino acids with various metal ions
Immobilised metal ion affinity chromatography (Imac) has shown great potential in selective binding and purification of polyhistidine-tagged recombinant proteins and peptides Purification of phosphopeptides, glycopeptides and metal binding proteins can also be performed using the Imac method
This article was originally published on Laboratorytalk on 23 Sep 2004 at 8.00am (UK)
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Columns for sample clean-up
Clean-up DNA, RNA, protein, peptides, and nucleotide preparation, quickly and easily with the Harvard Apparatus Gel Filtration (Sephadex) SpinColumns
Imac is based on the specific coordinate covalent binding between histidine or other metal binding amino acids (either naturally present on the surface of the protein or grafted) with various metal ions, such as copper, nickel, zinc, or iron immobilised or chelated to a polymeric binder or resin.
The bound sample can be eluted from the resin by reducing the pH, increasing the ionic strength or by including EDTA or imidazole in the elution buffer.
Since target protein can be enriched from a large volume of crude lysate in a single step, Imac purification offers significant time savings over less selective multi-step procedures.
Harvard Apparatus offers two convenient ready-to-use Imac formats: single sample SpinColumns and 96-well SpinColumns which allow processing of single or multiple samples in volumes from 10ul to 150ul.
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